Tripeptide Interference with Human Immunodeficiency Virus Type 1 Morphogenesis
(2002) In Antimicrobial Agents and Chemotherapy 46(11). p.3597-3605- Abstract
- 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... (More) - 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3516245
- author
- Höglund, Stefan ; Su, Jin ; Sandin-Reneby, Sara ; Végvári, Ákos LU ; Hjertén, Stellan ; Sintorn, Ida-Maria ; Foster, Hillary ; Wu, Yi-Pyng ; Nyström, Ingela and Vahlne, Anders
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Antimicrobial Agents and Chemotherapy
- volume
- 46
- issue
- 11
- pages
- 3597 - 3605
- publisher
- American Society for Microbiology
- external identifiers
-
- scopus:0036841348
- ISSN
- 1098-6596
- DOI
- 10.1128/AAC.46.11.3597-3605.2002
- language
- English
- LU publication?
- no
- id
- 25637ccc-eaaf-4103-8694-9288c9231d95 (old id 3516245)
- date added to LUP
- 2016-04-04 09:39:13
- date last changed
- 2022-03-23 06:35:50
@article{25637ccc-eaaf-4103-8694-9288c9231d95, abstract = {{Capsid assembly during virus replication is a potential target for antiviral therapy. The Gag polyprotein is<br/><br> the main structural component of retroviral particles, and in human immunodeficiency virus type 1 (HIV-1),<br/><br> it contains the sequences for the matrix, capsid, nucleocapsid, and several small polypeptides. Here, we report<br/><br> that at a concentration of 100 M, 7 of 83 tripeptide amides from the carboxyl-terminal sequence of the HIV-1<br/><br> 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.}}, author = {{Höglund, Stefan and Su, Jin and Sandin-Reneby, Sara and Végvári, Ákos and Hjertén, Stellan and Sintorn, Ida-Maria and Foster, Hillary and Wu, Yi-Pyng and Nyström, Ingela and Vahlne, Anders}}, issn = {{1098-6596}}, language = {{eng}}, number = {{11}}, pages = {{3597--3605}}, publisher = {{American Society for Microbiology}}, series = {{Antimicrobial Agents and Chemotherapy}}, title = {{Tripeptide Interference with Human Immunodeficiency Virus Type 1 Morphogenesis}}, url = {{http://dx.doi.org/10.1128/AAC.46.11.3597-3605.2002}}, doi = {{10.1128/AAC.46.11.3597-3605.2002}}, volume = {{46}}, year = {{2002}}, }