LF f(17-41) modified [id=LAG0005]

Synonym: LfcinC modified ; Linear LfcinC

Producer Organism : Native Protein : Production Method :
Goat Lactoferrin (LF) Synthetic
Activity : Antiviral
Target Organisms :

Unavailable data

Description :
Production method: Synthetic.

Length : 25 Mass (Da): 3 013.27 Common Amino Acids : R
Isolectric Point : 11.97 Net Charge : 7 Absent Amino Acids : DEFHN
Basic Residues : 7 Acidic Residues : 0 Hydrophobic Residues : 5
Polar Residues : 9 Boman Index : -88.39 Hydropathy Index : -0.964
Aliphatic Index : 46.8 Instability Index : 0 Extinction Coefficient : 7115
Absorbance 280nm : 296.46

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)

 3 LAG0011  93.8%  ------YQWQRRMR-LGAPSIT------- 
 4 LAG0012 100.0%  --------WQRRMRKLGAPSIT------- 
 5 LAG0013  92.9%  --------WQRRM-KLGAPSIT------- 
 6 LAG0010  93.8%  ------YQWQRRM-KLGAPSIT------- 
 7 LAG0008 100.0%  ------YQWQRRMRKLGAPSIT------- 
 8 LAG0009  93.8%  ------YQWQR-MRKLGAPSIT------- 


11 LAG0002 100.0%  ---SKCYQWQRRMRKLGA----------- 
12 LAG0003  93.3%  ---SKCYQWQWRMRKLGA----------- 

13 LAG0007 100.0%  ------YQWQRRMRKL------------- 

Citation: 1

Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts

Cited Entries: LFH0025, LAG0005

Authors:Andersen, J.H., Osbakk, S.A., Vorland, L.H., Traavik, T., Gutteberg, T.J.
Journal: Antiviral Research 2001, 51(2).
CrossRef External Link
Abstract: Lactoferrin is mainly produced by polymorphonuclear leukocytes and has been demonstrated in mammalian milk and external secretions. Lactoferrin is an iron-binding, multifunctional protein and may play an important role in immune regulation and in defense mechanisms against bacteria, fungi and viruses. Lactoferricin is a potent antimicrobial peptide generated from the N-terminal part of lactoferrin by pepsin cleavage. We demonstrate that lactoferrins from different species and its N-terminal peptide lactoferricin (particularly the cyclic form) inhibit expression of early and late antigens, as well as production of infectious viral progeny during human cytomegalovirus (HCMV) infection in vitro. Iron-saturated lactoferrin did not affect HCMV antigen expression. Heparin had the same effects as iron-depleted lactoferrin. Yet, mixtures of lactoferrin and heparin did not inhibit HCMV multiplication i.e. lactoferrin and heparin seemed to mutually block each other's antiviral activities. HCMV-infected cells exposed to lactoferrin and cyclic lactoferricin contained less intracellular virus than unexposed cells. The antiviral activity of cyclic lactoferricin was more than seven-fold weaker than that of the maternal molecule. Lactoferrin and cyclic lactoferricin prevented HCMV entrance into the host cell.
Keywords: Human cytomegalovirus (HCMV); Lactoferrin; Lactoferricin

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