Sequence similarity between the erythrocyte binding domain of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals a functional heparin binding motif involved in binding to the Duffy antigen receptor for chemokines
Author:
Publisher
Springer Science and Business Media LLC
Subject
Infectious Diseases,Virology
Link
http://link.springer.com/content/pdf/10.1186/1743-422X-8-523.pdf
Reference37 articles.
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2. Harrowe G, Cheng-Mayer C: Amino acid substitutions in the V3 loop are responsible for adaptation to growth in transformed T-cell lines of a primary human immunodeficiency virus type 1. Virol 1995, 210: 490-494. 10.1006/viro.1995.1367
3. Briggs TDLSJWGMM: Envelope V3 amino acid sequence predicts HIV-1 phenotype (co-receptor usage and tropism for macrophages). Aids 2000.
4. Shimizu N, Haraguchi Y, Takeuchi Y, Soda Y, Kanbe K, Hoshino H: Changes in and discrepancies between cell tropisms and coreceptor uses of human immunodeficiency virus type 1 induced by single point mutations at the V3 tip of the env protein. Virol 1999, 259: 324-333. 10.1006/viro.1999.9764
5. Callahan LN, Phelan M, Mallinson M, Norcross MA: Dextran sulfate blocks antibody binding to the principal neutralizing domain of human immunodeficiency virus type 1 without interfering with gp120-CD4 interactions. J Virol 1991, 65: 1543-1550.
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