Journal ArticleDOI
Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
William I. Weis,Jerry H. Brown,Stephen Cusack,Stephen Cusack,James C. Paulson,John J. Skehel,Don C. Wiley +6 more
TLDR
The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites, suggesting that antibodies neutralize virus infectivity by preventing virus-to-cell binding.Abstract:
The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites. Sialic acid fills the conserved pocket, demonstrating that it is the influenza virus receptor. The proximity of the antibody-binding sites suggests that antibodies neutralize virus infectivity by preventing virus-to-cell binding. The structures suggest approaches to the design of anti-viral drugs that could block attachment of viruses to cells.read more
Citations
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Antiviral therapy of influenza.
TL;DR: This review presents the current status of antiviral therapy of, and highlights the challenges presented by, the threat of pandemic influenza.
Optical Biosensors for Diagnostics of Infectious Viral Disease: A Recent Update
Atul Sharma,Rupesh K. Mishra,K. Yugender Goud,Mona A. Mohamed,Shekher Kummari,Swapnil Tiwari,Zhanhong Li,Roger J. Narayan,Lia Stanciu,Jean-Louis Marty +9 more
TL;DR: In this article, a review of the development and development of optical biosensors is presented, highlighting the existing challenges engaged in converting laboratory research to real-world device applications and optical diagnostics methods for virus infections.
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The Host Response to Influenza A Virus Interferes with SARS-CoV-2 Replication during Coinfection
TL;DR: The interaction between SARS-CoV-2 USA-WA1/2020 and influenza H1N1 A/California/04/2009 virus during coinfection is investigated and it is demonstrated that the host response to influenza A virus uniquely interferes with SARS/IAV biology although the inverse relationship is not evident.
Journal ArticleDOI
Multivalent glycans for biological and biomedical applications.
TL;DR: A recent review as discussed by the authors discusses recent advances made in the development and biological and biomedical applications of synthetic multivalent glycans, including neoglycopeptides, neoglycoproteins, glycodendrimers, glycopolymers, glyconanoparticles and glycoliposomes.
Journal ArticleDOI
Infectious Progeny of 2009 A (H1N1) Influenza Virus Replicated in and Released from Human Neutrophils
Zhang Zhang,Tao Huang,Feiyuan Yu,Xingmu Liu,Conghui Zhao,Xueling Chen,David J. Kelvin,Jiang Gu,Jiang Gu +8 more
TL;DR: It is found that human neutrophils in vitro without detectable level of sialic acid expression could be infected by this virus strain 2009 A (H1N1) influenza virus and it is shown that the infected neutrophil can not only synthesize 2009 A(H1n1) viral mRNA and proteins, but also produce infectious progeny.
References
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Journal ArticleDOI
The thiobarbituric acid assay of sialic acids.
TL;DR: This chapter discusses the different aspects of thiobarbituric acid assay of sialic acid, which is suitable for measuring the release of bound sialoic acid by sialidase and hydrolysis of sIALic acid-containing material must be carried out for the measurement of total sialsic acids.
Journal ArticleDOI
Areas, volumes, packing and protein structure.
TL;DR: This review is concerned with the packing of groups of atoms in proteins and with the area of solvent-protein interfaces.
Journal ArticleDOI
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
Journal ArticleDOI
Aromatic-aromatic interaction: a mechanism of protein structure stabilization
TL;DR: Analysis of neighboring aromatic groups in four biphenyl peptides or peptide analogs and 34 proteins reveals a specific aromatic-aromatic interaction that helps stabilize tertiary structure, and 20 percent stabilize quaternary structure.
Journal ArticleDOI
Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
TL;DR: Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified and at least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.
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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
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