The hemagglutinin structure of an avian H1N1 influenza A virus

• Published in: Virology (New York, N.Y.) Vol. 392; no. 1; pp. 73 - 81
• Main Authors: Lin, Tianwei, Wang, Gengyan, Li, Anzhang, Zhang, Qian, Wu, Caiming, Zhang, Rongfu, Cai, Qixu, Song, Wenjun, Yuen, Kwok-Yung
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.09.2009
• Subjects: Amino Acid Sequence; amino acid sequences; Animals; Base Sequence; BASIC BIOLOGICAL SCIENCES; Binding Sites; BIRDS; Birds - virology; Carbohydrate Sequence; chemistry; crystal structure; CRYSTALLOGRAPHY; Crystallography, X-Ray; DNA Primers; DNA Primers - genetics; galactose; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; genetics; glycosidic linkages; Glycosylation; H1N1; Hemagglutinin; Hemagglutinin Glycoproteins, Influenza Virus; Hemagglutinin Glycoproteins, Influenza Virus - chemistry; Hemagglutinin Glycoproteins, Influenza Virus - genetics; HEMAGGLUTININS; host-pathogen relationships; human diseases; human health; Humans; In Vitro Techniques; Infectious Disease; Influenza; Influenza A virus; Influenza A Virus, H1N1 Subtype; Influenza A Virus, H1N1 Subtype - chemistry; Influenza A Virus, H1N1 Subtype - genetics; INFLUENZA VIRUSES; lignads; Mammals; Models, Molecular; molecular models; Molecular Sequence Data; Molecular Structure; MORPHOLOGY; pathogenesis; polypeptides; polysaccharides; protein folding; protein structure; Protein Structure, Quaternary; Receptor; RECEPTORS; Receptors, Virus; Receptors, Virus - chemistry; Sequence Homology, Amino Acid; sialic acids; sialyllactose; Species Specificity; Static Electricity; Structure; virology; virus receptors; Structure; Hemagglutinin; Receptor; H1N1; Influenza
• ISSN: 0042-6822; 1096-0341; 1096-0341
• DOI: 10.1016/j.virol.2009.06.028

The interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaα2,3Gal glycosidic linkage over those with Siaα2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin.