Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein

<p>The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1. Although the full sequence was not found, a DSP sequence was located near the critical arginin...

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Main Author: Michael Andrew Meyer
Format: Article
Language:English
Published: MDPI AG 2013-07-01
Series:Neurology International
Subjects:
Online Access:http://www.pagepress.org/journals/index.php/ni/article/view/4854
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spelling doaj-0129330b012048eb9b82f564fd3e22aa2021-01-02T13:10:49ZengMDPI AGNeurology International2035-83852035-83772013-07-0153e14e1410.4081/ni.2013.e142569Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat proteinMichael Andrew Meyer0Department of Neurology, Tennova Health Care, Knoxville, TN<p>The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1. Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3). For the JC polyoma virus, a DSP sequence was found at residues 70, 71 and 72 with homology also noted for the mouse polyoma virus and SV40 virus. Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.</p>http://www.pagepress.org/journals/index.php/ni/article/view/4854JC, polyoma, virus, VP1, capsid, alpha 4 integrin, PML
collection DOAJ
language English
format Article
sources DOAJ
author Michael Andrew Meyer
spellingShingle Michael Andrew Meyer
Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein
Neurology International
JC, polyoma, virus, VP1, capsid, alpha 4 integrin, PML
author_facet Michael Andrew Meyer
author_sort Michael Andrew Meyer
title Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein
title_short Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein
title_full Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein
title_fullStr Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein
title_full_unstemmed Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein
title_sort amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous dsp sequence found for jc polyoma vp1 coat protein
publisher MDPI AG
series Neurology International
issn 2035-8385
2035-8377
publishDate 2013-07-01
description <p>The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1. Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3). For the JC polyoma virus, a DSP sequence was found at residues 70, 71 and 72 with homology also noted for the mouse polyoma virus and SV40 virus. Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.</p>
topic JC, polyoma, virus, VP1, capsid, alpha 4 integrin, PML
url http://www.pagepress.org/journals/index.php/ni/article/view/4854
work_keys_str_mv AT michaelandrewmeyer aminoacidsequencesmediatingvascularcelladhesionmolecule1bindingtointegrinalpha4homologousdspsequencefoundforjcpolyomavp1coatprotein
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