Epstein-Barr Virus Glycoprotein gB and gHgL Can Mediate Fusion and Entry in trans, and Heat Can Act as a Partial Surrogate for gHgL and Trigger a Conformational Change in gB

作者: L. S. Chesnokova , M. K. Ahuja , L. M. Hutt-Fletcher

DOI: 10.1128/JVI.01597-14

关键词: GlycoproteinCell biologyIntegrinCell fusionVirusMolecular biologyCell cultureEpstein–Barr virusB cellBiologyProteolytic enzymes

摘要: ABSTRACT Epstein-Barr virus (EBV) fusion with an epithelial cell requires glycoproteins gHgL and gB is triggered by interaction between integrin αvβ5, αvβ6, or αvβ8. Fusion a B gHgL, gp42, gp42 human leukocyte antigen class II. We report here that, like alpha- betaherpesviruses, EBV, gammaherpesvirus, can mediate if are expressed in trans . Entry of gH-null into possible the expresses entry same virus, which phenotypically lacks expressing presence soluble integrin. Heat capable inducing cells only gB, proteolytic digestion pattern virions changes way following exposure to heat integrins. It suggested that Gibbs free energy released as result high-affinity contributes activation required cause refolding from prefusion postfusion conformation. IMPORTANCE The core machinery herpesviruses consists gHgL. demonstrate betaherpesvirus, gammaherpesvirus EBV when opposing membranes, implicating interactions ectodomains proteins fusion. further show integrin, both activate fusion, possibly representing its

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