New insights into influenza A specificity: an evolution of paradigms

Ji, Yiqin; White, Yohanna Jb; Hadden, Jodi A.; Grant, Oliver C.; Woods, Robert J.

doi:10.1016/j.sbi.2017.06.001

Cited by 36 publications

(46 citation statements)

References 123 publications

(160 reference statements)

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“…Within the human host, changes in HA and NA activity resulting from antigenic drift may require functional coadaptation of HA and NA to restore the balance. This may be achieved by tuning the receptor (fine-)specificity and affinity of HA [61] and the activity of NA. Of note, all NA proteins preferentially cleave avian-over human-type receptors, although NA of human viruses cleaves human-type receptors relatively more efficiently [62,63].…”

Section: Glossarymentioning

confidence: 99%

Influenza A Virus Hemagglutinin–Neuraminidase–Receptor Balance: Preserving Virus Motility

Vries

Guo

et al. 2020

Trends in Microbiology

140

138

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Section: Glossarymentioning

confidence: 99%

Influenza A Virus Hemagglutinin–Neuraminidase–Receptor Balance: Preserving Virus Motility

Vries

Guo

et al. 2020

Trends in Microbiology

140

138

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“…However, such data still cannot explain the potential host factor(s) leading to host adaption of A(H3N8) from horses to dogs. Internal complexity of glycan structures below the sialic acid can influence glycan interaction with HA (25,26); thus, host adaption cannot be understood without first understanding the glycan substructures of Neu5Gc␣2,3Gal. The data from the isoform microarray and biolayer interferometry analyses demonstrated clear patterns of A(H3N8) CIV binding on a set of glycans with fucosylated ␣2,3-linked glycans (Fig.…”

Section: Figmentioning

confidence: 99%

Mutation W222L at the Receptor Binding Site of Hemagglutinin Could Facilitate Viral Adaption from Equine Influenza A(H3N8) Virus to Dogs

Wen

Blackmon

Olivier

et al. 2018

J Virol

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An outbreak of respiratory disease caused by the equine-origin influenza A(H3N8) virus was first detected in dogs in 2004 and since then has been enzootic among dogs. Currently, the molecular mechanisms underlying host adaption of this virus from horses to dogs is unknown. Here, we have applied quantitative binding, growth kinetics, and immunofluorescence analyses to elucidate these mechanisms. Our findings suggest that a substitution of W222L in the hemagglutinin of the equine-origin A(H3N8) virus facilitated its host adaption to dogs. This mutation increased binding avidity of the virus specifically to receptor glycans with -glycolylneuraminic acid (Neu5Gc) and sialyl Lewis X (SLe) motifs. We have demonstrated these motifs are abundantly located in the submucosal glands of dog trachea. Our findings also suggest that in addition to the type of glycosidic linkage (e.g., α2,3-linkage or α2,6-linkage), the type of sialic acid (Neu5Gc or 5--acetyl neuraminic acid) and the glycan substructure (e.g., SLe) also play an important role in host tropism of influenza A viruses. Influenza A viruses (IAVs) cause a significant burden on human and animal health, and mechanisms for interspecies transmission of IAVs are far from being understood. Findings from this study suggest that an equine-origin A(H3N8) IAV with mutation W222L at its hemagglutinin increased binding to canine-specific receptors with sialyl Lewis X and Neu5Gc motifs and, thereby, may have facilitated viral adaption from horses to dogs. These findings suggest that in addition to the glycosidic linkage (e.g., α2,3-linked and α2,6-linked), the substructure in the receptor saccharides (e.g., sialyl Lewis X and Neu5Gc) could present an interspecies transmission barrier for IAVs and drive viral mutations to overcome such barriers.

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“…α‐2,6‐sialyllactose and synthetic sialylated compounds with α‐2,6‐linked sialic acid also inhibit mycoplasma binding and gliding but require higher concentrations to do so, indicating a lower binding affinity (Roberts et al, ; Kasai et al, ). Thus, M. pneumoniae receptor specificity is somewhat nuanced with regard to sialic acid linkages, which is particularly significant in vivo, where diverse sialic acid linkages and other modifications are common, and in this respect M. pneumoniae recognition of sialylated receptors is similar to that of influenza virus hemagglutinin (Ji et al, ).…”

Section: Introductionmentioning

confidence: 99%

Sialylated Receptor Setting Influences Mycoplasma pneumoniae Attachment and Gliding Motility

Williams

Chen

Driver

et al. 2018

Molecular Microbiology

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Mycoplasma pneumoniae is a common cause of human respiratory tract infections, including bronchitis and atypical pneumonia. M. pneumoniae binds glycoprotein receptors having terminal sialic acid residues via the P1 adhesin protein. Here, we explored the impact of sialic acid presentation on M. pneumoniae adherence and gliding on surfaces coated with sialylated glycoproteins, or chemically functionalized with α-2,3- and α-2,6-sialyllactose ligated individually or in combination to a polymer scaffold in precisely controlled densities. In both models, gliding required a higher receptor density threshold than adherence, and receptor density influenced gliding frequency but not gliding speed. However, very high densities of α-2,3-sialyllactose actually reduced gliding frequency over peak levels observed at lower densities. Both α-2,3- and α-2,6-sialyllactose supported M. pneumoniae adherence, but gliding was only observed on the former. Finally, gliding on α-2,3-sialyllactose was inhibited on surfaces also conjugated with α-2,6-sialyllactose, suggesting that both moieties bind P1 despite the inability of the latter to support gliding. Our results indicate that the nature and density of host receptor moieties profoundly influences M. pneumoniae gliding, which could affect pathogenesis and infection outcome. Furthermore, precise functionalization of polymer scaffolds shows great promise for further analysis of sialic acid presentation and M. pneumoniae adherence and gliding.

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New insights into influenza A specificity: an evolution of paradigms

Cited by 36 publications

References 123 publications

Influenza A Virus Hemagglutinin–Neuraminidase–Receptor Balance: Preserving Virus Motility

Influenza A Virus Hemagglutinin–Neuraminidase–Receptor Balance: Preserving Virus Motility

Mutation W222L at the Receptor Binding Site of Hemagglutinin Could Facilitate Viral Adaption from Equine Influenza A(H3N8) Virus to Dogs

Sialylated Receptor Setting Influences Mycoplasma pneumoniae Attachment and Gliding Motility

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