A metastable form of the large envelope protein of duck hepatitis B virus: Low-pH release results in a transition to a hydrophobic, potentially fusogenic conformation

Journal of Virology

Volumn 74, Issue 11, 2000, Pages 5116-5122

  Grgacic, E V L ^a   Schaller, H ^b  

^a MACFARLANE BURNET INSTITUTE FOR MEDICAL RESEARCH AND PUBLIC HEALTH   (Australia)

^b UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DITHIOTHREITOL; LIPOSOME; TRYPSIN; VIRUS ENVELOPE PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HEAT; HEPATITIS B VIRUS; HYDROPHOBICITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; VIRUS CELL INTERACTION; VIRUS INACTIVATION; VIRUS PARTICLE;

ANIMALS; BINDING SITES; DITHIOTHREITOL; DUCKS; HEATING; HEPATITIS B VIRUS, DUCK; HYDROGEN-ION CONCENTRATION; LIPOSOMES; PROTEIN CONFORMATION; TRYPSIN; VIRAL ENVELOPE PROTEINS; VIRION;

EID: 0034063446     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.11.5116-5122.2000     Document Type: Article

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