<?xml version="1.0" encoding="UTF-8"?>
<article article-type="research-article" xml:lang="en" xmlns:xlink="http://www.w3.org/1999/xlink">
<front>
<journal-meta>
<journal-id journal-id-type="publisher">global-journal-of-science-frontier-research-c-biological-science</journal-id>
<journal-title-group>
<journal-title>Global Journal of Science Frontier Research - C: Biological Science</journal-title>
</journal-title-group>
<issn publication-format="print">0975-5896</issn>
<issn publication-format="electronic">2249-4626</issn>
<publisher><publisher-name>Global Journals Publishing Group Incorporated</publisher-name></publisher>
<self-uri xlink:href="https://globaljournals.org/journal-seo-export/jats/89644.xml" />
</journal-meta>
<article-meta>
<article-id pub-id-type="publisher-id">89644</article-id>
<title-group>
<article-title>HIV-1 Matrix Protein p17 Initiates Virus Assembly</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author"><name><surname>Bukrinskaya</surname><given-names>Alissa</given-names></name><xref ref-type="aff" rid="aff1" />
</contrib>
</contrib-group>
<aff id="aff1">RUSSIA, D.I. Ivanovsky Institute of Virology, Moscow, Russia</aff>
<pub-date publication-format="electronic" date-type="pub" iso-8601-date="2013-12-04">
<day>04</day>
<month>12</month>
<year>2013</year>
</pub-date>
<volume>13</volume>
<issue>C7</issue>
<fpage>21</fpage>
<lpage>22</lpage>
<abstract><p>HIV-1 matrix protein (MA) is the small multifunctional protein located on N terminus of Gag protein p55. MA posseses three transport signals: membranotropic, nucleophilic and the signal of nuclear export and functions in the cell as shuttle protein. MA is cleaved from Gag precursor by viral protease early in infection and is transported into the nuclei where it associates with viral RNA (vRNA). The complex MA-vRNA is transported to plasma membrane â€“ the place of HIV assembly - using MA membranotropic signal and phosphorilation. Mutant MA (M4) prepared by Dr. Dupont (USA, Worchester, Medical School) used in association with vRNA lost membranotropic signal and can not move to the plasma membrane. It was located in the nuclei and cytoskeleton. It could be suggested that mutant MA â€get stuckâ€ during cellular transport. That localization unusual for wild HIV-1 could suggest that wild MA complex with vRNA delivers vRNA from the nucleus to the plasma membrane through cytoskeleton.</p></abstract>
<self-uri content-type="pdf" xlink:href="https://globaljournals.org/GJSFR_Volume13/4-Hiv-1-Matrix-Protein.pdf" />
<self-uri content-type="html" xlink:href="https://globaljournals.org/scholarly-articles/hiv-1-matrix-protein-p17-initiates-virus-assembly/" />
</article-meta>
</front>
<body>
<sec>
<title>Full Text</title>
<p>HIV-1 matrix protein (MA) is the small multifunctional protein located on N terminus of Gag protein p55. MA posseses three transport signals: membranotropic, nucleophilic and the signal of nuclear export and functions in the cell as shuttle protein. MA is cleaved from Gag precursor by viral protease early in infection and is transported into the nuclei where it associates with viral RNA (vRNA). The complex MA-vRNA is transported to plasma membrane â€“ the place of HIV assembly - using  MA membranotropic signal and phosphorilation. Mutant MA (M4) prepared by Dr. Dupont (USA, Worchester, Medical School) used in association with vRNA lost membranotropic signal and can not move to the plasma membrane. It was located in the nuclei and cytoskeleton. It could be suggested that  mutant MA â€get stuckâ€ during cellular transport. That localization unusual for wild HIV-1 could suggest that wild MA complex with vRNA  delivers vRNA from the nucleus to the plasma membrane through cytoskeleton.</p>
</sec>
</body>
</article>