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Tripeptide Interference with Human Immunodeficiency Virus Type 1 Morphogenesis

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 (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)
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author
publishing date
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
2013-02-25 10:57:27
date last changed
2017-01-01 07:52:50
@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 (&gt;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},
  volume       = {46},
  year         = {2002},
}