Premium
A novel modified peptide derived from membrane‐proximal external region of human immunodeficiency virus type 1 envelope significantly enhances retrovirus infection
Author(s) -
Zhang Lishuang,
Jiang Chunlai,
Zhang Huayan,
Gong Xin,
Yang Lan,
Miao Liang,
Shi Yuhua,
Zhang Yan,
Kong Wei,
Zhang Chuntao,
Shan Yaming
Publication year - 2014
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2587
Subject(s) - peptide , gp41 , retrovirus , transduction (biophysics) , infectivity , residue (chemistry) , transmembrane protein , virology , virus , chemistry , glycoprotein , gene delivery , viral envelope , biology , gene , transfection , biochemistry , receptor , antibody , epitope , immunology
Efficient gene transfer is a critical goal in retroviral transduction. Several peptides capable of forming amyloid fibrils, such as the 39‐residue semen‐derived infection‐enhancing peptide (SEVI), have demonstrated the ability to boost retroviral gene delivery. Here, a 13‐residue peptide P13 (Ac‐ 671 NWFDITNWLWYIK 683 ) derived from the membrane‐proximal external region of the human immunodeficiency virus type 1 (HIV‐1) gp41 transmembrane protein, together with its 16‐residue peptide derivative (P16) were found to enhance HIV‐1 infection significantly. Both peptides, P13 and P16, could form amyloid fibril structures to potently enhance HIV‐1 infectivity. Further investigations showed that both aromatic Trp residues and cationic Lys residues contributed to the enhancement of HIV‐1 infection by these two active peptides. P16 could more effectively augment HIV‐1 YU‐2 infection than SEVI, implying its potential applications as a tool in the lab to improve gene transfer rates. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.