VP1 residues around the five-fold axis of enterovirus A71 mediate heparan sulfate interaction

Virology

Volumn 501, Issue , 2017, Pages 79-87

  Tan, Chee Wah ^a   Sam, I Ching ^a   Lee, Vannajan Sanghiran ^a,b   Wong, Hui Vern ^a   Chan, Yoke Fun ^a  

^a UNIVERSITY OF MALAYA   (Malaysia)

^b CHIANG MAI UNIVERSITY   (Thailand)

Author keywords

Enterovirus A71; Five fold axis; Hand, foot and mouth disease; Heparan sulfate

Indexed keywords

HEPARAN SULFATE; LYSINE; SEPHAROSE; UNCLASSIFIED DRUG; VIRAL PROTEIN; VIRAL PROTEIN 1; PROTEIN BINDING; VIRUS RECEPTOR;

AMINO ACID ANALYSIS; AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING SITE; CELL CULTURE; CONTROLLED STUDY; ENTEROVIRUS 71; GENE MUTATION; GENETIC PLASTICITY; GENETIC VARIABILITY; HUMAN; HUMAN CELL; IN VITRO STUDY; MOLECULAR DOCKING; MUTAGENESIS; MUTANT; NEXT GENERATION SEQUENCING; NONHUMAN; PHENOTYPE; PLASTICITY; PRIORITY JOURNAL; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; TISSUE CULTURE; VIRUS STRAIN; VP1 GENE; AMINO ACID SEQUENCE; ENTEROVIRUS A; ENTEROVIRUS INFECTION; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; VIROLOGY;

AMINO ACID SEQUENCE; BASE SEQUENCE; ENTEROVIRUS A, HUMAN; ENTEROVIRUS INFECTIONS; HEPARITIN SULFATE; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; RECEPTORS, VIRUS; VIRAL PROTEINS;

EID: 84995877456     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2016.11.009     Document Type: Article

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