Abstract
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.
Highlights
The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies ly to the IDSP sequence which mediates binding of VLA-4 to vascular cell n adhesion molecule 1
Three dimensional modeling of the VP1 molecule suggests that rc the DSP loop has an accessible site for interaction from the external side of the assembled e viral capsid pentamer. omm Introduction -c Administration of an antibody to the alpha 4 integrin molecule binding site to the head region of the vascular cell o adhesion molecule 1 (VCAM-1) molecule was N found to be associated with systemic JC
Since IDSP is a critical VCAM-1 amino acid sequence for binding to the alpha 4 integrin,[5] a search was made to find a similar sequence in the VP1 protein that could mediate an attachment to integrins
Summary
The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies ly to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell n adhesion molecule 1.
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