Tripeptide Interference with Human Immunodeficiency Virus Type 1 Morphogenesis
Författare
Summary, in English
Capsid assembly during virus replication is a potential target for antiviral therapy. The Gag polyprotein is
the main structural component of retroviral particles, and in human immunodeficiency virus type 1 (HIV-1),
it contains the sequences for the matrix, capsid, nucleocapsid, and several small polypeptides. Here, we report
that at a concentration of 100 M, 7 of 83 tripeptide amides from the carboxyl-terminal sequence of the HIV-1
capsid protein p24 suppressed HIV-1 replication (>80%). The three most potent tripeptides, glycyl-prolylglycine-amide (GPG-NH2), alanyl-leucyl-glycine-amide (ALG-NH2), and arginyl-glutaminyl-glycine-amide (RQG-NH2), were found to interact with p24. With electron microscopy, disarranged core structures of HIV-1 progeny were extensively observed when the cells were treated with GPG-NH2 and ALG-NH2. Furthermore, nodular structures of approximately the same size as the broad end of HIV-1 conical capsids were observed at the plasma membranes of treated cells only, possibly indicating an arrest of the budding process. Corresponding tripeptides with nonamidated carboxyl termini were not biologically active and did not interact with p24.
the main structural component of retroviral particles, and in human immunodeficiency virus type 1 (HIV-1),
it contains the sequences for the matrix, capsid, nucleocapsid, and several small polypeptides. Here, we report
that at a concentration of 100 M, 7 of 83 tripeptide amides from the carboxyl-terminal sequence of the HIV-1
capsid protein p24 suppressed HIV-1 replication (>80%). The three most potent tripeptides, glycyl-prolylglycine-amide (GPG-NH2), alanyl-leucyl-glycine-amide (ALG-NH2), and arginyl-glutaminyl-glycine-amide (RQG-NH2), were found to interact with p24. With electron microscopy, disarranged core structures of HIV-1 progeny were extensively observed when the cells were treated with GPG-NH2 and ALG-NH2. Furthermore, nodular structures of approximately the same size as the broad end of HIV-1 conical capsids were observed at the plasma membranes of treated cells only, possibly indicating an arrest of the budding process. Corresponding tripeptides with nonamidated carboxyl termini were not biologically active and did not interact with p24.
Publiceringsår
2002
Språk
Engelska
Sidor
3597-3605
Publikation/Tidskrift/Serie
Antimicrobial Agents and Chemotherapy
Volym
46
Issue
11
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
American Society for Microbiology
Ämne
- Medical Engineering
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1098-6596