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Different HIV‐1 env frames: gp120 and ASP (antisense protein) biosynthesis, and theirs co‐variation tropic amino acid signatures in X4‐ and R5‐viruses
Author(s) -
Dimonte Salvatore
Publication year - 2017
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.24611
Subject(s) - tropism , biology , amino acid , virology , gene , mutation , virus , tissue tropism , genetics , human immunodeficiency virus (hiv) , dendrogram , computational biology , genetic diversity , medicine , population , environmental health
Antisense protein (ASP) is the new actor of viral life of Human Immunodeficiency Virus type 1 (HIV‐1) although proposed above 20 years ago. The asp ORF is into complementary strand of the gp120/gp41 junction of env gene. The ASP biological role remains little known. Knowing the Env markers of viral tropism, a dataset of sequences (660 strains) was used to analyze the hypothetical ASP involvement in CCR5 (R5) and/or CXCR4 (X4) co‐receptor interaction. Preliminarily, prevalence of ASP and gp120 V3 mutations was performed; following association among mutations were elaborate. The classical V3 tropic‐signatures were confirmed, and 36 R5‐ and 22 X4‐tropic ASP mutations were found. Moreover, by analyzing the ASP sequences, 36 out of 179 amino acid positions significantly associated with different co‐receptor usage were found. Several statistically significant associations between gp120 V3 and ASP mutations were observed. The dendrogram showed the existence of a cluster associated with R5‐usage and a large cluster associated with X4‐usage. These results show that gp120 V3 and specific amino acid changes in ASP are associated together with CXCR4 and/or CCR5‐usage. These findings implement previous observations on unclear ASP functions. J. Med. Virol. 89:112–122, 2017 . © 2016 Wiley Periodicals, Inc.