The Antisense Protein ASP of HIV-1 Enhances Viral Entry in CD4+ T Cells

The negative strand of the human immunodeficiency virus-1 (HIV-1) proviral genome contains an antisense open reading frame encoding a protein (ASP) with no known homologs. The presence of immune responses to ASP in people living with HIV-1 (PLWH) demonstrates its expression in vivo. Further, the predicted hydrophobicity of ASP is consistent with its association with the plasma membrane and viral envelope. Despite this body of evidence, the role of ASP in HIV-1 replication remains unknown. In this report, we investigated the hypothesis that the presence of ASP on the viral surface enhances HIV-1 entry into target cells. We generated an ASP-knockout replication-competent HIV-1 molecular clone in the NL4-3 background, which we used to perform cell-cell fusion, viral entry, and viral replication assays. Our results suggest that the presence of ASP on the plasma membrane of infected cells and the envelope of HIV-1 virions enhances viral transmission. Overall, our studies provide first evidence that ASP plays a role in the HIV-1 replication cycle. Further investigation into these observations may lead to the identification of new HIV-1 vulnerabilities that may be the target of novel interventions.

Authors

Institutions

Publication Details

Journal
Viruses
Published
2025-09-30
DOI
https://doi.org/10.3390/v17101332
Citations
2
Primary Topic
HIV Research and Treatment
Type
article
Field-Weighted Citation Impact
2.07

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

The Antisense Protein ASP of HIV-1 Enhances Viral Entry in CD4+ T Cells

Fabio Romerio, Nathalie Chazal, Jean-Michel Mesnard, Isabella Caico et al.
2 citations
Viruses
HIV Research and Treatment
2.07
article

The Antisense Protein ASP of HIV-1 Enhances Viral Entry in CD4+ T Cells

Fabio Romerio, Nathalie Chazal, Jean-Michel Mesnard, Isabella Caico, Lucile Espert, Aurélie Rivault, Myriam Abla Houmey
article en
2 citations

Abstract

The negative strand of the human immunodeficiency virus-1 (HIV-1) proviral genome contains an antisense open reading frame encoding a protein (ASP) with no known homologs. The presence of immune responses to ASP in people living with HIV-1 (PLWH) demonstrates its expression in vivo. Further, the predicted hydrophobicity of ASP is consistent with its association with the plasma membrane and viral envelope. Despite this body of evidence, the role of ASP in HIV-1 replication remains unknown. In this report, we investigated the hypothesis that the presence of ASP on the viral surface enhances HIV-1 entry into target cells. We generated an ASP-knockout replication-competent HIV-1 molecular clone in the NL4-3 background, which we used to perform cell-cell fusion, viral entry, and viral replication assays. Our results suggest that the presence of ASP on the plasma membrane of infected cells and the envelope of HIV-1 virions enhances viral transmission. Overall, our studies provide first evidence that ASP plays a role in the HIV-1 replication cycle. Further investigation into these observations may lead to the identification of new HIV-1 vulnerabilities that may be the target of novel interventions.

VirusesVol. 17(10)
Centre National de la Recherche Scientifique (FR), Johns Hopkins University (US), Johns Hopkins Medicine (US), Institut de Recherche en Infectiologie de Montpellier (FR)
Styrelsen för Internationellt Utvecklingssamarbete, Sidaction, Agence Nationale de Recherches sur le Sida et les Hépatites Virales, Centre National de la Recherche Scientifique, Université de Montpellier
Openalex Percentile: Top 12%
HIV Research and Treatment
2.07
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.