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
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DissertationDOI
Molecular biology of host - influenza virus nucleoprotein (NP) interactions and their relevance in the pathogenesis of influenza virus.
TL;DR: A novel strategy adopted by IAV for utilizing the much conserved ubiquitin proteasomal pathway is described and a promising host target for antiviral intervention is unraveled.
Posted Content
Algorithmic Bio-surveillance For Precise Spatio-temporal Prediction of Zoonotic Emergence.
TL;DR: Machine inference is used to demonstrate a high accuracy predictive bio-surveillance capability, designed to pro-actively localize an impending species jump via automated interrogation of massive sequence databases of viral proteins, and shows that the inverse classification accuracy is a quantitative indicator of jump risk.
Journal ArticleDOI
Triplet entropy analysis of hemagglutinin and neuraminidase sequences measures influenza virus phylodynamics.
Günther J.L. Gerhardt,Agnes A.S. Takeda,Tahila Andrighetti,Ivaine T.S. Sartor,Sergio Echeverrigaray,Scheila de Avila e Silva,Laurita dos Santos,José Luiz Rybarczyk-Filho +7 more
TL;DR: This work presents triplet entropy analysis as a potential phylodynamic tool to quantify nucleotide organization of viral sequences and shows that differentiation in entropy precedes differentiation in GC content for both groups.
Reference EntryDOI
Virus–Host Cell Interactions
TL;DR: This chapter discusses virus–host cell interactions, cytopathic effect (CPE), poisson distribution, cytocidal infections, and effects on Host-Cell Metabolism.
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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