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Lactoferricin B [id=LFB0084]

Synonym: LF f(17-41) ; LFcin B

Producer Organism : Native Protein : Production Method :
Cow Lactoferrin (LF) Enzymatic hydrolysis and Purification with LC method
Activity : Antibacterial, antifungal, antiparasitical
Target Organisms :

Gram-positive: Bacillus subtilis NBRC 3134 (no MIC), Bacillus subtilis ATCC 6633 (MIC=0.6-2 g/ml), Bacillus subtilis 2116 (MIC=7.8 g/ml), Bacillus subtilis IFO-3009 (MIC=2 g/ml), Bacillus cereus MMI-272 (MIC=9 g/ml), Bacillus cereus 6349 (MIC=15.6 g/ml), Bacillus circulans JCM-2504T (MIC=0.6 g/ml), Bacillus sphaericus 7585 (MIC=1.9 g/ml), Staphylococcus aureus JCM-2151 (MIC=6-25 g/ml or MIC=2-3M), Staphylococcus aureus JCM-2179 (MIC=6 g/ml), Staphylococcus aureus JCM-2413 (MIC=18 g/ml), Staphylococcus aureus ATCC 25923 (MIC=30 g/ml), Staphylococcus aureus ATCC 29213 (MIC=6.6 g/ml), Staphylococcus aureus 8530 (MIC=15.6 g/ml), Staphylococcus aureus 8532 (MIC=15.6 g/ml), Staphylococcus aureus R1 (antibiotic-resistant) (MIC=12 g/ml), Staphylococcus epidermidis JCM-2414T (MIC=3-6 g/ml), Staphylococcus epidermidis 4276 (MIC=7.8 g/ml), Staphylococcus haemolyticus JCM-2416T (MIC=1 g/ml), Staphylococcus hominus JCM-2419T (MIC=3 g/ml), Staphylococcus sp. wild type (MIC=7.8-15.6 g/ml), Listeria monocytogenes IDF-Ib (MIC=0.3 M or MIC=0.6g/ml), Listeria monocytogenes JCM-7673 (MIC=1 g/ml), Listeria monocytogenes JCM-7674 (MIC=3 g/ml), Listeria monocytogenes EGD (MIC=1.6 g/ml), Listeria monocytogenes 4b (MIC=6.6 g/ml), Listeria monocytogenes 5105 (MIC=1.9 g/ml), Streptococcus bovis JCM-5672 (MIC=3-6 g/ml), Streptococcus mutans JCM-5705T (MIC=6 g/ml), Streptococcus mutans JCM-5175 (MIC=6 g/ml), Streptococcus mutans JCM-5176 (MIC=3 g/ml), Streptococcus thermophilus ATCC-19258 (MIC=3 g/ml), Streptococcus lactis ATCC-19435 (MIC=3 g/ml), Streptococcus cremoris ATCC-9265 (MIC=3 g/ml), Lactobacillus casei MMI-114 (MIC=12 g/ml), Corynebacterium ammoniagenes JCM-1306 (MIC=0.3 g/ml), Corynebacterium renale JCM-1322 (MIC=1 g/ml), Corynebacterium diphtheriae JCM-1310 (MIC=18 g/ml), Clostridium perfringens ATCC-6013 (MIC=24 g/ml), Clostridium paraputrificum MMI-25 (MIC=3 g/ml or MIC>60 g/ml), Micrococcus sp. wild type (MIC=7.8-31.25 g/ml), Bifidobacterium adolescentis ATCC-15703 (no MIC), Bifidobacterium breve ATCC-15700 (no MIC), Bifidobacterium longum ATCG15707 (no MIC), Bifidobacterium infantis ATCC-15697 (no MIC).

Gram-negative: Escherichia coli NBRC 3301 (no MIC), Escherichia coli IID-861 (MIC=6-50 g/ml or MIC=2 M), Escherichia coli ATCC 25922 (MIC=3.3-30 g/ml), Escherichia coli O111 (MIC=6-12 g/ml or LC50=12 g/ml), Escherichia coli O157:H7-A (MIC=8 g/ml), Escherichia coli O157:H7-B (MIC=8 g/ml), Escherichia coli O157:H7-C (MIC=10 g/ml), Escherichia coli O157:H7-D (MIC=8 g/ml), Escherichia coli O157 wild type (MIC=7.8 g/ml), Escherichia coli CL99 1-2 (MIC=4 g/ml), Escherichia coli K12 UB1005 (MIC=1.6 g/ml), Escherichia coli K12 UB1005 DC-2 (MIC=1.6 g/ml), Escherichia coli 7275 (MIC=7.8 g/ml), Escherichia coli 10418 (MIC=3.9 g/ml), Escherichia coli wild type (MIC=15.6-31.25 g/ml), Pseudomonas aeruginosa MMI-603 (MIC=12-24 g/ml), Pseudomonas aeruginosa IFO-3445 (MIC=12-18 g/ml or MIC>200 g/ml), Pseudomonas aeruginosa IFO-3446 (MIC=24 g/ml or MIC=2 M), Pseudomonas aeruginosa IFO-3448 (MIC=45 g/ml), Pseudomonas aeruginosa IFO-3452 (MIC=30 g/ml), Pseudomonas aeruginosa ATCC-2783 (MIC=3.3 g/ml), Pseudomonas aeruginosa PAO (MIC=3.3 g/ml), Pseudomonas aeruginosa 10662 (MIC=31.25 g/ml), Pseudomonas aeruginosa wild type (MIC=15.6-31.25 g/ml), Pseudomonas putida wild type (MIC=15.6 g/ml), Pseudomonas cepacia wild type (MIC=250-500 g/ml), Pseudomonas fluorescens wild type (MIC=15.6 g/ml), Salmonella enteritidis IID-604 (MIC=12-18 g/ml), Salmonella typhimurium SH7641 (MIC=1.6 g/ml), Salmonella typhimurium SL696 (MIC=5 g/ml), Salmonella typhimurium 6749 (MIC=1.6 g/ml), Salmonella montevideo SL5222 (MIC=3 g/ml), Salmonella newport 5751 (MIC=7.8 g/ml), Salmonella typhi wild type (MIC=7.8-15.6 g/ml), Salmonella enteritidis wild type (MIC=7.8 g/ml), Yersinia enterocolitica IID-981 (MIC=6-24 g/ml), Yersinia enterocolitica wild type (MIC=62.5 g/ml), Proteus vulgaris JCM 1668T (MIC=12-45 g/ml), Proteus vulgaris wild type (MIC=500 g/ml), Proteus mirabilis wild type (MIC=250-500 g/ml), Proteus rettgeri wild type (MIC=250 g/ml), Proteus sp. wild type (MIC=500 g/ml), Klebsiella pneumoniae JCM 1662T (MIC=9 g/ml or MIC=3 M), Klebsiella pneumoniae JCM-16623 (MIC=12 g/ml), Klebsiella pneumoniae 5055 (MIC=15.6 g/ml), Klebsiella pneumoniae wild type (MIC=15.6-62.5 g/ml), Shigella flexneri 5452 (MIC=3.9 g/ml), Shigella flexneri wild type (MIC=3.9 g/ml), Shigella sonnei wild type (MIC=7.8 g/ml), Enterococcus sp. wild type (MIC=62.5-125 g/ml), Enterobacter intermedius wild type (MIC=15.6 g/ml), Enterobacter aerogenes wild type (MIC=125 g/ml), Enterobacter cloacae wild type (MIC=70.3 g/ml), Enterobacter sp. wild type (MIC=7.8 g/ml), Serratia liquefaciens wild type (MIC=500 g/ml), Citrobacter freundii wild type (MIC=7.8-62.5 g/ml), Citrobacter diversus wild type (MIC=62.5 g/ml), Bacteroides distasonis MMI-M602 (no MIC), Bacteroides vulgatus MMI-S601 (no MIC), Campylobacter jejuni JCM-2013 (no MIC).

Yeast: Candida albicans TIMM 0154 (MIC=25 g/ml), Candida albicans TIMM 1768 (MIC=12.5-400 g/ml), Candida albicans TIMM 3164 (MIC=400 g/ml), Candida albicans TIMM 3315 (MIC=50 g/ml), Candida albicans TIMM 3317 (MIC=200 g/ml), Candida albicans JCM1542T (MIC=24 g/ml), Candida albicans JCM2072 (MIC=30 g/ml), Candida albicans JCM2075 (MIC=45 g/ml), Candida albicans JCM2076 (MIC=24 g/ml), Candida albicans JCM2374 (MIC=24 g/ml), Candida albicans JCM2900 (MIC=24 g/ml), Candida albicans JCM2901 (MIC=45 g/ml), Candida albicans JCM2902 (MIC=60 g/ml), Candida albicans JCM2904 (MIC=45 g/ml), Candida albicans 6372 (MIC=0.8 g/ml), Candida albicans 6434 (MIC=0.8 g/ml), Candida albicans ATCC 90028 (MIC=400 g/ml), Candida albicans wild type (MIC=7.8-21.67 g/ml), Candida parapsilosis wild type (MIC=7.8-80 g/ml), Candida tropicalis (MIC=0.31-1.25 g/ml), Candida glabrata (MIC=120 g/ml), Candida guilliermondii (MIC=5-40 g/ml), Candida kefyr (MIC=2.5-10 g/ml), Candida krusei (MIC=10-20 g/ml), Cryptococcus uniguttulatus JCM 3685 (MIC=6 g/ml), Cryptococcus curvatus JCM 1532T (MIC=9 g/ml), Cryptococcus albidus JCM 8252 (MIC=24 g/ml), Cryptococcus neoformans (MIC=0.63 g/ml), Trichosporon cutaneum JCM 2466 (MIC=18 g/ml), Trichosporon cutaneum (MIC=1.25-2.5 g/ml), Saccharomyces cerevisiae (MIC=0.63 g/ml).

Filamentous fungi: Trichophyton mentagrophytes TIMM 1189 (MIC=12 g/ml), Trichophyton mentagrophytes TIMM 2789 (MIC=6.3 g/ml), Trichophyton mentagrophytes IFO 5466 (MIC=30 g/ml), Trichophyton mentagrophytes IFO 5812 (MIC=30 g/ml), Trichophyton mentagrophytes IFO 5974 (MIC=45 g/ml), Trichophyton mentagrophytes (MIC=5 g/ml or MIC>80 g/m), Trichophyton rubrum IFO 6203 (MIC=24 g/ml), Trichophyton rubrum IFO 32409 (MIC=13 g/ml), Trichophyton tonsurans (MIC=5-40 g/ml), Trichophyton violaceum (MIC=40 g/ml or MIC>80 g/m), Nannizzia incurvata JCM 1906 (MIC=18 g/ml), Nannizzia otae JCM 1909 (MIC=60 g/ml), Penicillium pinophilum JCM 5593 (MIC=45 g/ml), Penicillium vermiculatum JCM 5595 (MIC=45 g/ml), Aspergillus versicolor (MIC=10 g/ml), Fusarium moniliforme (MIC=2.5-5 g/ml), Absidia corymbifera (MIC=40 g/ml or MIC>80 g/m), Microsporum canis (MIC=40 g/ml), Microsporum gypseum (MIC=20-40 g/ml), Epidermophyton floccosum (MIC=0.31-2.5 g/ml), Fonsecaea pedrosoi (MIC=5 g/ml), Exophiala dermatitidis (MIC=2 g/ml), Phialophora verrucosa (MIC=5-10 g/ml), Cladosporium trichoides (MIC=5 g/ml), Paracoccidioides brasiliensis (MIC=0.63-1.25 g/ml), Sporothrix schenckii (MIC=2-10 g/ml).

Parasite: Giardia lamblia (LD50=2.8 M).

NOTE: No activity against Bifidobacterium bifidum ATCC-15696 (>60 M), Enterococcus faecalis ATCCE 19433 (>60 g/ml), Proteus mirabilis NCTC-60 (>200 g/ml), Proteus mirabilis ATCC 35659 (>1000 g/ml), Pseudomonas fluorescens IFO-14160 (>60 g/ml), Proteus vulgaris 4635, Klebsiella pneumoniae 418, Serratia marcescens wild type, Serratia sp. wild type (500 g/ml), Rhizopus oryzae JCM 5557, Nannizzia gypsea JCM 1903, Aspergillus fumigatus JCM 1917, Aspergillus niger JCM 5546 (>60 g/ml), Aspergillus fumigatus, Aspergillus niger, Aspergillus flavus, Aspergillus clavatus, Penicillium notatum, Penicillium expansum, Mucor circinelloides, Mucor racemosus, Rhizopus oryzae, Trichophyton rubrum, Trichophyton shoenleinii (>80 g/ml) .

Description :
Production method: Pepsin hydrolysis and purification with LC method. The origin of the pepsin is not indicated.

See LFB0085, LFB0086 and LFB0087.
Length : 25 Mass (Da): 3 126.25 Common Amino Acids : R
Isolectric Point : 12.35 Net Charge : 8 Absent Amino Acids : DEHNY
Basic Residues : 8 Acidic Residues : 0 Hydrophobic Residues : 9
Polar Residues : 5 Boman Index : -68.79 Hydropathy Index : -0.576
Aliphatic Index : 50.8 Instability Index : 0 Extinction Coefficient : 11125
Absorbance 280nm : 463.54

Wheel representation

Hydrophobicity plot

Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).
Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).
Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

Multiple Sequence Alignment (MSA)


                      1 [        .         .         . ] 32
  1 LFBNATIVE 100.0%    FKCRRWQWRMKKLGAPSITCVRRAFALECIRA   
  2 LFB0017   100.0%    FKCRRWQWR-----------------------   
  3 LFB0043    93.3%    FKCRRWQWRAKKLGA-----------------   
  4 LFB0052    86.7%    FKCWRWQWRWKKLGA-----------------   
  5 LFB0037    93.3%    FKCARWQWRMKKLGA-----------------   
  6 LFB0040    93.3%    FKCRRWAWRMKKLGA-----------------   
  7 LFB0038    93.3%    FKCRAWQWRMKKLGA-----------------   
  8 LFB0088    96.0%    FKCRRWQWRMKKLGAPSITCVRRAE-------   
  9 LFB0039    93.3%    FKCRRAQWRMKKLGA-----------------   
 10 LFB0062    93.3%    FKCRRAQWRMKKLGA-----------------   
 11 LFB0072    93.3%    FKCRRAQWRMKKLGA-----------------   
 12 LFB0075    93.3%    FKCRRAQWRMKKLGA-----------------   
 13 LFB0078    93.3%    FKCRRAQWRMKKLGA-----------------   
 14 LFB0064    86.7%    FKCRRAQARMKKLGA-----------------   
 15 LFB0117    54.5%    ---RRAAARAKKAG------------------   
 16 LFB0080    86.7%    FKCRRAQARMKKLGA-----------------   
 17 LFB0074    86.7%    FKCRRAQARMKKLGA-----------------   
 18 LFB0077    86.7%    FKCRRAQARMKKLGA-----------------   
 19 LFB0056    93.3%    FKCRRFQWRMKKLGA-----------------   
 20 LFB0059    93.3%    FKCRRFQWRMKKLGA-----------------   
 21 LFB0053    93.3%    FKCRRFQWRMKKLGA-----------------   
 22 LFB0081    93.3%    FKCRRFQWRMKKLGA-----------------   
 23 LFB0055    86.7%    FKCRRFQFRMKKLGA-----------------   
 24 LFB0058    86.7%    FKCRRFQFRMKKLGA-----------------   
 25 LFB0061    86.7%    FKCRRFQFRMKKLGA-----------------   
 26 LFB0083    86.7%    FKCRRFQFRMKKLGA-----------------   
 27 LFB0041    93.3%    FKCRRWQARMKKLGA-----------------   
 28 LFB0063    93.3%    FKCRRWQARMKKLGA-----------------   
 29 LFB0076    93.3%    FKCRRWQARMKKLGA-----------------   
 30 LFB0079    93.3%    FKCRRWQARMKKLGA-----------------   
 31 LFB0073    93.3%    FKCRRWQARMKKLGA-----------------   
 32 LFB0060    93.3%    FKCRRWQFRMKKLGA-----------------   
 33 LFB0082    93.3%    FKCRRWQFRMKKLGA-----------------   
 34 LFB0057    93.3%    FKCRRWQFRMKKLGA-----------------   
 35 LFB0054    93.3%    FKCRRWQFRMKKLGA-----------------   
 36 LFB0042    93.3%    FKCRRWQWAMKKLGA-----------------   
 37 LFB0115    81.8%    ---RRWQRWMKKLG------------------   
 38 LFB0033   100.0%    FKCRRWQWRMKKLGA-----------------   
 39 LFB0032   100.0%    FKCRRWQWRMKKLGA-----------------   
 40 LFB0031   100.0%    FKCRRWQWRMKKLGA-----------------   
 41 LFB0050    86.7%    FKWRRWQWRMKKLWA-----------------   
 42 LFB0051    80.0%    FKWRRWWWRMKKLWA-----------------   
 43 LFB0049    93.3%    FKCRRWQWRMKKLWA-----------------   
 44 LFB0018   100.0%    FKCRRWQWRM----------------------   
 45 LFB0020   100.0%    FKCRRWQWRMK---------------------   
 46 LFB0045    93.3%    FKCRRWQWRMKALGA-----------------   
 47 LFB0044    93.3%    FKCRRWQWRMAKLGA-----------------   
 48 LFB0097   100.0%    ---RRWQWR-----------------------   
 49 LFB0030   100.0%    FKCRRWQWRMKKLG------------------   
 50 LFB0087   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 51 LFB0024    54.5%    YKAWRWAWRWK---------------------   
 52 LFB0025    54.5%    YKAWRWAWRWK---------------------   
 53 LFB0027    36.4%    YRMWRWAWRWR---------------------   
 54 LFB0028    36.4%    YRMWRWRWRWR---------------------   
 55 LFB0026    36.4%    YRAWRWAWRWR---------------------   
 56 LFB0023    63.6%    YKARRWAWRWK---------------------   
 57 LFB0022    72.7%    YKARRWAWRMK---------------------   
 58 LFB0021    81.8%    FKARRWAWRMK---------------------   
 59 LFB0019    90.0%    FKARRWQWRM----------------------   
 60 LFB0036    93.3%    FKARRWQWRMKKLGA-----------------   
 61 LFB0070    93.3%    FKARRWQWRMKKLGA-----------------   
 62 LFB0069    93.3%    FKARRWQWRMKKLGA-----------------   
 63 LFB0068    93.3%    FKARRWQWRMKKLGA-----------------   
 64 LFB0065    93.3%    FKARRWQWRMKKLGA-----------------   
 65 LFB0106   100.0%    ---RRWQWRMKK--------------------   
 66 LFB0029    45.5%    RRWYRWAWRMR---------------------   
 67 LFB0118   100.0%    ----RWQWRM----------------------   
 68 LFB0113    81.8%    ---RRWQWRMRRLG------------------   
 69 LFB0112    72.7%    ---KKWQWKMKKLG------------------   
 70 LFB0114    81.8%    ---KKWQWRMKKLG------------------   
 71 LFB0116    54.5%    ---EEWQWEMEELG------------------   
 72 LFB0048    93.3%    FKWRRWQWRMKKLGA-----------------   
 73 LFB0090    92.0%    FKSRRWQWRMKKLGAPSITSVRRAF-------   
 74 LFB0110    18.2%    ----RRWQWRMKKLG-----------------   
 75 LFB0067    93.3%    FKFRRWQWRMKKLGA-----------------   
 76 LFB0071    93.3%    FKFRRWQWRMKKLGA-----------------   
 77 LFB0066    93.3%    FKFRRWQWRMKKLGA-----------------   
 78 LFB0108   100.0%    ---RRWQWRMKKL-------------------   
 79 LFB0102   100.0%    ---RRWQWRMKK--------------------   
 80 LFB0034    93.3%    AKCRRWQWRMKKLGA-----------------   
 81 LFB0111   100.0%    ---RRWQWRMKKLG------------------   
 82 LFB0104   100.0%    ---RRWQWRMKK--------------------   
 83 LFB0035    93.3%    FACRRWQWRMKKLGA-----------------   
 84 LFB0109   100.0%    ---RRWQWRMKKLG------------------   
 85 LFB0101   100.0%    ---RRWQWRMKK--------------------   
 86 LFB0046    93.3%    FKCRRWQWRMKKAGA-----------------   
 87 LFB0107   100.0%    ---RRWQWRMKK--------------------   
 88 LFB0100   100.0%    ---RRWQWRMKK--------------------   
 89 LFB0047    93.3%    FKCRRWQWRMKKLAA-----------------   
 90 LFB0098   100.0%    ---RRWQWRMKK--------------------   
 91 LFB0105   100.0%    ---RRWQWRMKK--------------------   
 92 LFB0103   100.0%    ---RRWQWRMKK--------------------   
 93 LFB0086   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 94 LFB0089   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 95 LFB0085   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 96 LFB0084   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 97 LFB0092   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFA------   
 98 LFB0095   100.0%    -KCRRWQWRMKKLGAPSITCV-----------   
 99 LFB0096   100.0%    --CRRWQWRMKKLGAPSITCV-----------   

100 LFB0093   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFAL-----   

101 LFB0091   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFA------   

102 LFB0119   100.0%    ----------KKLGAPSITCVRRAFA------   
103 LFB0120   100.0%    -------------GAPSITCVRRAF-------   

104 LFB0121   100.0%    ----------------------------CIRA   
105 LFB0094   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFALECIR-   

Citation: 1

Antifungal properties of lactoferricin B, a peptide derived from the N-terminal region of bovine lactoferrin

Cited Entries: LFB0084

Authors:Bellamy, W., Yamauchi, K., Wakabayashi, H., Takase, M., Takakura, N., Shimamura, S., Tomita, M.
Journal: Letters in Applied Microbiology 1994, 18(4).
Abstract: A number of yeasts and filamentous fungi, including agents of skin disease (dermatophytes), were tested and found to be susceptible to inhibition by lactoferricin B. Effective concentrations varied within the range of 3 to 60 μg ml-1, depending on the strain and culture medium used. Lactoferricin B inhibited fungal uptake of 3H-glucose with effectiveness similar to polymyxin B, suggesting that it may target the cell membrane. It caused a profound change in ultrastructural features of the dermatophyte Trichophyton mentagrophytes.
Citation: 2

Lactoferricin, a new antimicrobial peptide

Cited Entries: LFB0084

Authors:Jones, E., Smart, A., Bloomberg, G., Burgess, L., Millar, M.
Journal: Journal of Applied Microbiology 1994, 77(2).
Abstract: Lactoferricin B (LF-B) is a peptide derived from acid-pepsin digestion of bovine lactoferrin, which has antimicrobial properties. In order to assess the antimicrobial spectrum of LF-B and its possible in vivo uses, the minimum inhibitory and microbicidal concentrations of pure lactoferricin B were determined for a range of bacterial species and under varying conditions of growth including growth phase and size of the inoculum, pH and ionic strength of the medium. Lactoferricin B was bactericidal against a wide range of bacteria and Candida albicans. Proteus spp., Pseudomonas cepacia and Serratia spp. were resistant. The bactericidal activity of LF-B was inhibited by increasing ionic strength and bacterial inoculum and at acid pH. The activity of lactoferricin B was completely inhibited by the addition of 5% whole cow's milk and was reduced in the presence of increasing concentrations of mucin. These results indicate the potential of LF-B to reduce the numbers of organisms in a simple medium, but raise doubts about its role in vivo because of its sensitivity to changes in physical variables. It may be that lactoferricin exerts a transient antimicrobial effect at mucosal surfaces.
Citation: 3

Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin

Cited Entries: LFB0084, LFB0089

Authors:Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K., Tomita, M.
Journal: Journal of Applied Microbiology 1992, 73(6).
Abstract: A physiologically diverse range of Gram-positive and Gram-negative bacteria was found to be susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by gastric pepsin digestion of bovine lactoferrin. The list of susceptible organisms includes Escherichia coli, Salmonella enteritidis, Klebsiella pneumoniae, Proteus vulgaris, Yersinia enterocolitica, Pseudomonas aeruginosa, Campylobacter jejuni, Staphylococcus aureus, Streptococcus mutans, Corynebacterium diphtheriae, Listeria monocytogenes and Clostridium perfringens. Concentrations of lactoferricin B required to cause complete inhibition of growth varied within the range of 0.3 to 150 micrograms/ml, depending on the strain and the culture medium used. The peptide showed activity against E. coli O111 over the range of pH 5.5 to 7.5 and was most effective under slightly alkaline conditions. Its antibacterial effectiveness was reduced in the presence of Na+, K+, Mg2+ or Ca2+ ions, or in the presence of various buffer salts. Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested. Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.
Citation: 4

Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin

Cited Entries: LFB0084

Authors:Bellamy, W., Wakabayashi, H., Takase, M., Kawase, K., Shimamura, S., Tomita, M.
Journal: Medical Microbiology and Immunology 1993, 182(2).
Abstract: Candida albicans was found to be highly susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by enzymatic cleavage of bovine lactoferrin. Effective concentrations of the peptide varied within the range of 18 to 150 micrograms/ml depending on the strain and the culture medium used. Its effect was lethal, causing a rapid loss of colony-forming capability. 14C-labeled lactoferricin B bound to C. albicans and the rate of binding appeared to be consistent with the rate of killing induced by the peptide. The extent of binding was diminished in the presence of Mg2+ or Ca2+ ions which acted to reduce its anticandidal effectiveness. Binding occurred optimally at pH 6.0 and killing was maximal near the same pH. Such evidence suggests the lethal effect of lactoferricin B results from its direct interaction with the cell surface. Cells exposed to lactoferricin B exhibited profound ultrastructural damage which appeared to reflect its induction of an autolytic response. These findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans.
Keywords: Medicine
Citation: 5

Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment

Cited Entries: LFB0084

Authors:Yamauchi, K., Tomita, M., Giehl, T.J., Ellison, R.T., 3rd
Journal: Infection and Immunity 1993, 61(2).
Abstract: Although the antimicrobial activity of lactoferrin has been well described, its mechanism of action has been poorly characterized. Recent work has indicated that in addition to binding iron, human lactoferrin damages the outer membrane of gram-negative bacteria. In this study, we determined whether bovine lactoferrin and a pepsin-derived bovine lactoferrin peptide (lactoferricin) fragment have similar activities. We found that both 20 microM bovine lactoferrin and 20 microM lactoferricin release intrinsically labeled [3H]lipopolysaccharide ([3H]LPS) from three bacterial strains, Escherichia coli CL99 1-2, Salmonella typhimurium SL696, and Salmonella montevideo SL5222. Under most conditions, more LPS is released by the peptide fragment than by whole bovine lactoferrin. In the presence of either lactoferrin or lactoferricin there is increased killing of E. coli CL99 1-2 by lysozyme. Like human lactoferrin, bovine lactoferrin and lactoferricin have the ability to bind to free intrinsically labeled [3H]LPS molecules. In addition to these effects, whereas bovine lactoferrin was at most bacteriostatic, lactoferricin demonstrated consistent bactericidal activity against gram-negative bacteria. This bactericidal effect is modulated by the cations Ca2+, Mg2+, and Fe3+ but is independent of the osmolarity of the medium. Transmission electron microscopy of bacterial cells exposed to lactoferricin show the immediate development of electron-dense "membrane blisters." These experiments offer evidence that bovine lactoferrin and lactoferricin damage the outer membrane of gram-negative bacteria. Moreover, the peptide fragment lactoferricin has direct bactericidal activity. As lactoferrin is exposed to proteolytic factors in vivo which could cleave the lactoferricin fragment, the effects of this peptide are of both mechanistic and physiologic relevance.
Citation: 6

Giardicidal activity of lactoferrin and N-terminal peptides

Cited Entries: LFH0024, LFB0084

Authors:Turchany, J.M., Aley, S.B., Gillin, F.D.
Journal: Infection and Immunity 1995, 63(11).
Abstract: Human and bovine lactoferrins and their derived N-terminal peptides were giardicidal in vitro. Fe3+, but not Fe2+, protected trophozoites from both native lactoferrin and peptides, although the latter lack iron-binding sites. Other divalent metal ions protected only against native lactoferrin. Log-phase cells were more resistant to killing than stationary-phase cells. These studies suggest that lactoferrin, especially in the form of the N-terminal peptides, may be an important nonimmune component of host mucosal defenses against Giardia lamblia.
Citation: 7

Inhibition of hyphal growth of azole-resistant strains of Candida albicans by triazole antifungal agents in the presence of lactoferrin-related compounds

Cited Entries: LFB0084

Authors:Wakabayashi, H., Abe, S., Teraguchi, S., Hayasawa, H., Yamaguchi, H.
Journal: Antimicrobial Agents and Chemotherapy 1998, 42(7).
Abstract: The effects of bovine lactoferrin (LF) or the LF-derived antimicrobial peptide lactoferricin B (LFcin B) on the growth of Candida albicans hyphae, including those of three azole-resistant strains, were investigated by a crystal violet staining method. The hyphae of two highly azole-resistant strains were more susceptible to inhibition by LF or LFcin B than the azole-susceptible strains tested. One moderately azole-resistant strain was defective in the formation of hyphae and showed a susceptibility to LF greater than that of the susceptible strains but a susceptibility to LFcin B similar to that of the susceptible strains. The highly azole-resistant strain TIMM3317 showed trailing growth in the presence of fluconazole or itraconazole, while the extent of growth was reduced by the addition of LF or LFcin B at a sub-MIC. Thus, the addition of LF or LFcin B at a sub-MIC resulted in a substantial decrease in the MICs of fluconazole and itraconazole for two highly azole-resistant strains; e.g., the MIC of fluconazole for TIMM3317 was shifted from >256 to 0.25 {micro}g/ml by LF, but the MICs were not decreased for the susceptible strains. The combination effects observed with triazoles and LF-related compounds in the case of the two highly azole-resistant strains were confirmed to be synergistic by the fractional inhibitory concentration index. These results demonstrate that for some azole-resistant C. albicans strains, LF-related compounds combined with triazoles can inhibit the growth of hyphae, an important form of this organism in pathogenesis.
Citation: 8

Post-antibiotic effect of the antimicrobial peptide lactoferricin on Escherichia coli and Staphylococcus aureus

Cited Entries: LFB0031, LFB0032, LFB0033, LFB0084

Authors:Haukland, H.H., Vorland, L.H.
Journal: Journal of Antimicrobial Chemotherapy 2001, 48(4).
Abstract: Lactoferricin is an antimicrobial peptide generated by gastric pepsin cleavage of lactoferrin. A possible post-antibiotic effect (PAE) of bovine lactoferricin (Lfcin B) and two shorter peptide derivatives against Staphylococcus aureus and Escherichia coli was studied. A drug removal technique involving centrifugation and washing was used. No PAE was found for Lfcin B against these two bacteria. The shorter derivatives had a short PAE against E. coli. They had a short negative PAE against S. aureus. In conclusion, the overall PAE is not overwhelming, but the small differences found between the different peptideg"bacteria combinations could indicate that different peptide mechanisms of action might be present.
Citation: 9

Novel antibacterial lactoferrin peptides generated by rennet digestion and autofocusing technique

Cited Entries: LFB0011, LFB0084, LFB0110, LFB0111, LFB0122, LFB0152, LFB0153

Authors:Elbarbary, H.A., Abdou, A.M., Park, E.Y., Nakamura, Y., Mohamed, H.A., Sato, K.
Journal: International Dairy Journal 2010, 20(9).
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Abstract: Bovine lactoferrin was hydrolysed with a range of proteolytic enzymes including calf rennet, fungal rennin, and porcine pepsin. Lactoferrin hydrolysates were assessed for their antibacterial activities against Escherichia coli and Bacillus subtilis. At pH 3, calf rennet lactoferrin hydrolysate before (LFH) showed the highest antimicrobial activity, then pepsin LFH, while fungal rennin LFH was the least active. The calf rennet and pepsin LFH were fractionated using autofocusing and chromatographic techniques. The activity-guided fractionation of calf rennet LFH identified a potent antimicrobial peptide of 11-residues, lactoferricin B (Lf-cin B), and three other novel antibacterial peptides. The 11-residues Lf-cin B was the most potent antibacterial peptide and was isolated from both rennet and pepsin LFH. Pepsin LFH had a main antimicrobial peptide of 25-residues, which was not detected in calf rennet LFH. It could be concluded that calf rennet LFH had stronger antibacterial properties than porcine pepsin LFH. Besides, autofocusing could be used for scaling up the isolation of the potent rennet LFH peptides that would have a widespread commercial use as a natural food preservative substituting porcine pepsin digest, especially in Islamic communities.
Citation: 10

N-acylated and D enantiomer derivatives of a nonamer core peptide of lactoferricin B showing improved antimicrobial activity

Cited Entries: LFH0025, LFB0084, LFB0098, LFB0100, LFB0101, LFB0102, LFB0103, LFB0104, LFB0105, LFB0106, LFB0107

Authors:Wakabayashi, H., Matsumoto, H., Hashimoto, K., Teraguchi, S., Takase, M., Hayasawa, H.
Journal: Antimicrobial Agents and Chemotherapy 1999, 43(5).
Abstract: N-acylated or D enantiomer peptide derivatives based on the sequence RRWQWRMKK in lactoferricin B demonstrated antimicrobial activities greater than those of lactoferricin B against bacteria and fungi. The most potent peptide, conjugated with an 11-carbon-chain acyl group, showed two to eight times lower MIC than lactoferricin B.
Citation: 11

Identification of the bactericidal domain of lactoferrin

Cited Entries: LFH0009, LFH0024, LFB0084, LFB0089

Authors:Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K., Tomita, M.
Journal: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1992, 1121(1-2).
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Abstract: We report the existence of a previously unknown antimicrobial domain near the N-terminus of lactoferrin in a region distinct from its iron-binding sites. A single active peptide representing this domain was isolated following gastric pepsin cleavage of human lactoferrin, and bovine lactoferrin, and sequenced by automated Edman degradation. The antimicrobial sequence was found to consist mainly of a loop of 18 amino acid residues formed by a disulfide bond between cysteine residues 20 and 37 of human lactoferrin, or 19 and 36 of bovine lactoferrin. Synthetic analogs of this region similarly exhibited potent antibacterial properties. The active peptide of bovine lactoferrin was more potent than that of human lactoferrin having effectiveness against various Gram-negative and Gram-positive bacteria at concentrations between 0.3 μM and 3.0 μM, depending on the target strain. The effect of the isolated domain was lethal causing a rapid loss of colony-forming capability. Our studies suggest this domain is the structural region responsible for the bactericidal properties of lactoferrin.
Keywords: Lactoferrin; Bactericidal domain; antimicrobial peptide; Lactoferricin
Citation: 12

The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm

Cited Entries: LFB0031, LFB0032, LFB0033, LFB0084

Authors:Haukland, H.H., Ulvatne, H., Sandvik, K., Vorland, L.H.
Journal: FEBS Letters 2001, 508(3).
CrossRef External Link
Keywords: antimicrobial peptide; Lactoferricin; Magainin; Cecropin; Cytoplasmic membrane; Cytoplasm
Citation: 13

Antibacterial effects of lactoferricin B

Cited Entries: LFB0031, LFB0032, LFB0033, LFB0084

Authors:Vorland, L.H., Ulvatne, H., Andersen, J., Haukland, H.H., Rekdal, O., Svendsen, J.S., Gutteberg, T.J.
Journal: Scandinavian Journal of Infectious Diseases 1999, 31.
Abstract: The antimicrobial peptide, lactoferricin, can be generated upon gastric pepsin cleavage of lactoferrin. We have examined the inhibitory efficacy of lactoferricin of bovine origin (Lf-cin B) on Escherichia coli, Proteus mirabilis and Staphylococcus aureus with or without a cell wall. We found that spheroplasts and protoplasts had a lower MIC than their counterparts with a cell wall. We also compared the efficacies of Lf-cin B (17-31) made of all L-amino acids and all D-amino acids. The peptide made of all D-amino acids was more active than the corresponding L-enantiomer. Furthermore, we examined the influence of Lf-cin B on the motility of E. coli and the influence of temperature on the susceptibility of bacteria exposed to Lf-cin B. Bacteria exposed to sub-MIC of Lf-cin B lost their motility. Bacteria exposed to Lf-cin B at 20 degrees C were more sensitive to Lf-cin B than when exposed at 37 degrees C. These findings indicate that the cell envelope is a limiting step for Lf-cin B to exert its antibiotic effect. We cannot rule out a receptor-mediated first step for Lf-cin B (17-31).
Keywords: PEPTIDE antibiotics; ANTIBACTERIAL agents
Citation: 14

A review: The active peptide of lactoferrin

Cited Entries: LFH0024, LFB0084, LFB0089, LFB0097, LFB0178, LFB0179

Authors:Tomita, M., Takase, M., Bellamy, W., Shimamura, S.
Journal: Acta Paediatrica Japonica 1994, 36.
Abstract: A potent antimicrobial peptide, lactoferricin, was found to be generated upon gastric pepsin cleavage of lactoferrin. The active peptide consists mainly of a loop of 18 amino acid residues, derived from the N-terminal region of the lactoferrin molecule, Like various other antimicrobial peptides that display membrane-disruptive properties, it contains a high proportion of basic amino acid residues. A physiologically diverse range of micro-organisms was tested and found to be susceptible to inhibition by this natural peptide including Gram-negative and Gram-positive bacteria, yeasts and filamentous fungi. Its antimicrobial effect against sensitive micro-organisms was lethal. Electron microscopy studies revealed that it induces a profound change in cell ultrastructural features and causes substantial cell damage in bacteria and fungi. These findings suggest the possibility that active peptides of lactoferrin may have a role in the host defense against microbial disease. If produced in substantial quantities in vivo such peptides could have important physiological significance, especially in nursing infants.
Keywords: antimicrobial peptide, lactofemcin, lactoferrin, pepsin digestion.
Citation: 15

Antifungal spectrum and fungicidal mechanism of an N-terminal peptide of bovine lactoferrin

Cited Entries: LFB0084

Authors:Wakabayashi, H., Hiratani, T., Uchida, K., Yamaguchi, H.
Journal: Journal of Infection and Chemotherapy 1996, 1(3): 185-189.
Abstract: The antifungal spectrum and fungicidal mechanism of an N-terminal peptide of bovine lactoferrin (lactoferricin | B), an antimicrobial peptide produced by gastric pepsin digestion of bovine lactoferrin, were investigated. The susceptibility of pathogenic yeasts and dermatophytes to the peptide varied in a species-dependent and straindependent manner. Dematiaceous fungi and dimorphic fungi were susceptible to the peptide (range of MIC values: 0.63 to 10 #g/mL). In the case of nonpigmented hyphomycetes and zygomycetes, most strains exhibited resistance to the peptide (MIC: > 80 #g/mL). This peptide killed Candida albicans dose dependently without inducing a change in cell wall stability against osmotic stress. The peptide at 10 #g/ml immediately induced the release of K from C albicans cells and pH increases in cell suspensions. These pharmacological activities were more potent than those for miconazole nitrate, a well-known antifungal agent that interferes with membrane synthesis and function. These in vitro findings suggest that the lactoferrin oligopeptide has potent membrane disrupting activity against this yeast and suggests that in vivo LF-B studies would be useful to further understand host defenses and to develop improved therapeutic agents against yeast infections.
Keywords: lactoferrin; lactoferricin; Candida albicans; membrane disruption
Citation: 16

Antibacterial activity of bovine lactoferrin and its peptides against enterohaemorrhagic Escherichia coli O157:H7

Cited Entries: LFB0084

Authors:Shin, K., Yamauchi, K., Teraguchi, S., Hayasawa, H., Tomita, M., Otsuka, Y., Yamazaki, S.
Journal: Letters in Applied Microbiology 1998, 26(6): 407-411.
PubMed link
Abstract: The antimicrobial activities of bovine lactoferrin (bLF), its pepsin hydrolysate (bLFH) and the active peptide lactoferricin B (LFcinB) against four clinical isolates of enterohaemorrhagic Escherichia coli O157:H7 were studied. The MICs against these isolates were 3 mg ml-1 for bLF, 0.1-0.2 mg ml-1 for bLFH and 8-10 micrograms ml-1 for LFcinB in 1% Bactopeptone broth. LFcinB killed these bacteria within 3 h at concentrations above 10 micrograms ml-1. Transmission electron microscopy findings suggested that LFcinB acts on the bacterial surface and affects cytoplasmic contents. LFcinB was shown to influence the levels of verotoxins in the culture supernatant fluid of an E. coli O157:H7 strain. These results demonstrate that E. coli O157:H7 strains are susceptible to the antimicrobial effects of bLF and its peptides.
Keywords: Animals; Anti-Bacterial Agents/*pharmacology; Bacterial Toxins/analysis; Cattle; Cell Membrane/drug effects/ultrastructure; Cytoplasm/drug effects/ultrastructure; Escherichia coli O157/chemistry/*drug effects; Humans; Lactoferrin/*analogs & derivatives/*pharmacology; Microbial Sensitivity Tests; Microscopy, Electron; Peptide Fragments/*pharmacology

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