Importance of hemagglutinin glycosylation for the biological functions of influenza virus

Virus Research

Volumn 82, Issue 1-2, 2001, Pages 73-75

  Klenk, Hans Dieter ^a   Wagner, Ralf ^a   Heuer, Dagmar ^a   Wolff, Thorsten ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Hemagglutinin; Influenza virus; Neuraminidase

Indexed keywords

CARBOHYDRATE; HEMAGGLUTININ; MUTANT PROTEIN; OLIGOSACCHARIDE; PROTEINASE; SIALIDASE; VIRUS FUSION PROTEIN; VIRUS GLYCOPROTEIN;

AMINO TERMINAL SEQUENCE; BINDING SITE; CARBOHYDRATE ANALYSIS; CARBOXY TERMINAL SEQUENCE; CELL FUSION; CELL STRAIN; CONFORMATIONAL TRANSITION; ENDOCYTOSIS; ENDOSOME; GLYCOSYLATION; INFLUENZA VIRUS; LIFE CYCLE; NONHUMAN; PH; PRIORITY JOURNAL; PROGENY; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN STABILITY; RECEPTOR AFFINITY; RECEPTOR BINDING; SHORT SURVEY; TEMPERATURE SENSITIVITY; VIROGENESIS; VIRUS ASSEMBLY; VIRUS ENVELOPE; VIRUS MUTANT; VIRUS MUTATION; VIRUS RECOMBINANT; VIRUS REPLICATION; VIRUS TITRATION;

ANIMALS; GLYCOSYLATION; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HUMANS; N-ACETYLNEURAMINIC ACID; NEURAMINIDASE; ORTHOMYXOVIRIDAE; RECEPTORS, VIRUS;

INFLUENZA VIRUS;

EID: 0037196586     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1702(01)00389-6     Document Type: Review

References (3)

1. Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety
2. Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity
3. Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth - A study by reverse genetics