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

Journal of Virology

Volumn 88, Issue 21, 2014, Pages 12193-12201

  Chesnokova, Liudmila S ^a   Ahuja, Munish K ^a,b   Hutt Fletcher, Lindsey M ^a  

^a LOUISIANA STATE UNIVERSITY HEALTH SCIENCES CENTER   (United States)

^b NONE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAVBETA5 INTEGRIN; ALPHAVBETA6 INTEGRIN; ALPHAVBETA8 INTEGRIN; INTEGRIN; PROTEIN GB; PROTEIN GHGL; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; CHAPERONE; GLYCOPROTEIN 85, EPSTEIN-BARR VIRUS; GLYCOPROTEIN B, HUMAN HERPESVIRUS 4; GLYCOPROTEIN L, HUMAN HERPESVIRUS 4; MEMBRANE PROTEIN; VIRUS ENVELOPE PROTEIN; VIRUS PROTEIN;

ALPHAHERPESVIRINAE; ARTICLE; BETAHERPESVIRINAE; BINDING AFFINITY; CELL FUSION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; EPITHELIUM CELL; EPSTEIN BARR VIRUS; HEAT; HUMAN; HUMAN CELL; NONHUMAN; PHENOTYPE; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PURIFICATION; VIRION; VIRUS ENTRY; ANIMAL; B LYMPHOCYTE; CELL LINE; METABOLISM; PHYSIOLOGY; PROTEIN CONFORMATION; RADIATION RESPONSE; VIROLOGY;

ANIMALS; B-LYMPHOCYTES; CELL LINE; HERPESVIRUS 4, HUMAN; HOT TEMPERATURE; HUMANS; MEMBRANE GLYCOPROTEINS; MOLECULAR CHAPERONES; PROTEIN CONFORMATION; VIRAL ENVELOPE PROTEINS; VIRAL PROTEINS; VIRUS INTERNALIZATION;

EID: 84907996437     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01597-14     Document Type: Article

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