Abstract
The matrix (MA) protein of HIV-1 is the N-terminal component of the Gag structural protein and is critical for the early and late stages of viral replication. MA contains five α-helices (α1-α5). Deletions in the N-terminus of α5 as small as three amino acids impaired virus release. Electron microscopy of one deletion mutant (MAΔ96-120) showed that its particles were tethered to the surface of cells by membranous stalks. Immunoblots indicated all mutants were processed completely, but mutants with large deletions had alternative processing intermediates. Consistent with the EM data, MAΔ96-120 retained membrane association and multimerization capability. Co-expression of this mutant inhibited wild type particle release. Alanine scanning mutation in this region did not affect virus release, although the progeny virions were poorly infectious. Combined, these data demonstrate that structural ablation of the α5 of MA inhibits virus release.
| Original language | English |
|---|---|
| Pages (from-to) | 293-302 |
| Number of pages | 10 |
| Journal | Virology |
| Volume | 468 |
| DOIs | |
| State | Published - Nov 1 2014 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Virology
- Medicine(all)
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Deletions in the fifth alpha helix of HIV-1 matrix block virus release. / Sanford, Bridget; Li, Yan; Maly, Connor J.; Madson, Christian J.; Chen, Han; Zhou, You; Belshan, Michael A.
In: Virology, Vol. 468, 01.11.2014, p. 293-302.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Deletions in the fifth alpha helix of HIV-1 matrix block virus release
AU - Sanford, Bridget
AU - Li, Yan
AU - Maly, Connor J.
AU - Madson, Christian J.
AU - Chen, Han
AU - Zhou, You
AU - Belshan, Michael A.
PY - 2014/11/1
Y1 - 2014/11/1
N2 - The matrix (MA) protein of HIV-1 is the N-terminal component of the Gag structural protein and is critical for the early and late stages of viral replication. MA contains five α-helices (α1-α5). Deletions in the N-terminus of α5 as small as three amino acids impaired virus release. Electron microscopy of one deletion mutant (MAΔ96-120) showed that its particles were tethered to the surface of cells by membranous stalks. Immunoblots indicated all mutants were processed completely, but mutants with large deletions had alternative processing intermediates. Consistent with the EM data, MAΔ96-120 retained membrane association and multimerization capability. Co-expression of this mutant inhibited wild type particle release. Alanine scanning mutation in this region did not affect virus release, although the progeny virions were poorly infectious. Combined, these data demonstrate that structural ablation of the α5 of MA inhibits virus release.
AB - The matrix (MA) protein of HIV-1 is the N-terminal component of the Gag structural protein and is critical for the early and late stages of viral replication. MA contains five α-helices (α1-α5). Deletions in the N-terminus of α5 as small as three amino acids impaired virus release. Electron microscopy of one deletion mutant (MAΔ96-120) showed that its particles were tethered to the surface of cells by membranous stalks. Immunoblots indicated all mutants were processed completely, but mutants with large deletions had alternative processing intermediates. Consistent with the EM data, MAΔ96-120 retained membrane association and multimerization capability. Co-expression of this mutant inhibited wild type particle release. Alanine scanning mutation in this region did not affect virus release, although the progeny virions were poorly infectious. Combined, these data demonstrate that structural ablation of the α5 of MA inhibits virus release.
UR - http://www.scopus.com/inward/record.url?scp=84907466297&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84907466297&partnerID=8YFLogxK
U2 - 10.1016/j.virol.2014.08.017
DO - 10.1016/j.virol.2014.08.017
M3 - Article
C2 - 25217711
AN - SCOPUS:84907466297
VL - 468
SP - 293
EP - 302
JO - Virology
JF - Virology
SN - 0042-6822
ER -