4xc5
CRYSTAL STRUCTURE OF THE T1L REOVIRUS ATTACHMENT PROTEIN SIGMA1CRYSTAL STRUCTURE OF THE T1L REOVIRUS ATTACHMENT PROTEIN SIGMA1
Structural highlights
FunctionSIGM1_REOVL Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis (By similarity). Publication Abstract from PubMedMammalian orthoreoviruses use glycans and junctional adhesion molecule-A (JAM-A) as attachment receptors. We determined the structure of serotype 1 reovirus attachment protein sigma1 alone and in complex with JAM-A. Comparison with the structure of serotype 3 reovirus sigma1 bound to JAM-A reveals that both sigma1 proteins engage JAM-A with similar affinities and via conserved binding epitopes. Thus, sigma1-JAM-A interactions are unlikely to explain the differences in pathogenesis displayed by these reovirus serotypes. Structure of serotype 1 reovirus attachment protein sigma1 in complex with JAM-A reveals a conserved serotype-independent binding epitope.,Stettner E, Dietrich MH, Reiss K, Dermody TS, Stehle T J Virol. 2015 Mar 25. pii: JVI.00433-15. PMID:25810543[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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