Structure of HCMV glycoprotein B in the postfusion conformation bound to a neutralizing human antibody

Nature Communications

Volumn 6, Issue , 2015, Pages

  Chandramouli, Sumana ^a   Ciferri, Claudio ^a,e   Nikitin, Pavel A ^b   Caló, Stefano ^c   Gerrein, Rachel ^a   Balabanis, Kara ^a   Monroe, James ^a   Hebner, Christy ^b   Lilja, Anders E ^a,f   Settembre, Ethan C ^d   Carfi, Andrea ^a  

^a GLAXOSMITHKLINE   (United States)

^b Norvartis Institute for BioMedical Research   (United States)

^c GSK   (Italy)

^d NVS Influenza Vaccines   (United States)

^e GENENTECH INC   (United States)

^f HOOKIPA BIOTECH AG   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GLYCOPROTEIN B; HUMAN MONOCLONAL ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; NEUTRALIZING ANTIBODY; GLYCOPROTEIN B, SIMPLEXVIRUS; VIRUS ANTIBODY; VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN; VIRUS FUSION PROTEIN;

ANTIBODY; ANTIGEN; CRYSTAL STRUCTURE; INFECTIVITY; PROTEIN; VACCINE; VIRUS;

ANTIBODY RESPONSE; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DIMERIZATION; DISULFIDE BOND; GLYCOSYLATION; HEAVY CHAIN; HERPES SIMPLEX VIRUS; HUMAN; HUMAN CELL; HUMAN CYTOMEGALOVIRUS; HYDROGEN BOND; HYDROPHOBICITY; IMMUNOPRECIPITATION; LIGHT CHAIN; NONHUMAN; PEPTIDE MAPPING; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN POLYMORPHISM; PROTEIN SECRETION; SITE DIRECTED MUTAGENESIS; SURFACE AREA; SURFACE CHARGE; VIRION; VIRUS NEUTRALIZATION; CHEMISTRY; CYTOMEGALOVIRUS; ELECTRON MICROSCOPY; IMMUNOLOGY; METABOLISM; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

HERPESVIRIDAE; HUMAN HERPESVIRUS 5; SIMPLEXVIRUS;

ANTIBODIES, NEUTRALIZING; ANTIBODIES, VIRAL; ANTIGENS, VIRAL; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYTOMEGALOVIRUS; HUMANS; IMMUNOGLOBULIN FAB FRAGMENTS; IMMUNOPRECIPITATION; MICROSCOPY, ELECTRON; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; VIRAL ENVELOPE PROTEINS; VIRAL FUSION PROTEINS;

EID: 84941729631     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9176     Document Type: Article

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