HIV-1 Matrix Trimerization-Impaired Mutants Are Rescued by Matrix Substitutions That Enhance Envelope Glycoprotein Incorporation.

doi:10.1128/JVI.01526-19

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Community

Back to search

Article

HIV-1 Matrix Trimerization-Impaired Mutants Are Rescued by Matrix Substitutions That Enhance Envelope Glycoprotein Incorporation.

Journal of virology - 12 Dec 2019

Tedbury Philip R, Novikova Mariia, Alfadhli Ayna, Hikichi Yuta, Kagiampakis Ioannis, KewalRamani Vineet N, Barklis Eric, Freed Eric O

Abstract excerpt

The matrix (MA) domain of HIV-1 Gag plays key roles in virus assembly by targeting the Gag precursor to the plasma membrane and directing the incorporation of the viral envelope (Env) glycoprotein into virions. The latter function appears to be in part dependent on trimerization of the MA domain of Gag during assembly, as disruption of the MA trimer interface impairs Env incorporation. Conversely, many MA...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to env Gene Products, Human Immunodeficiency Virus
Share to gag Gene Products, Human Immunodeficiency Virus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Leukemia Virus, Murine

Share to Protein Conformation, alpha-Helical

Share to Protein Interaction Domains and Motifs

Share to Viral Matrix Proteins

Share to Virion

Share to Virus Assembly

Source

Open in PubMed Open full text

Identifiers

PMID: 31619553
DOI: 10.1128/JVI.01526-19
PMCID: PMC6912099

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.