Antigenic Pressure on H3N2 Influenza Virus Drift Strains Imposes Constraints on Binding to Sialylated Receptors but Not Phosphorylated Glycans

Byrd-Leotis, Lauren; Gao, Chao; Jia, Nan; Mehta, Akul Y.; Trost, Jessica F.; Cummings, Sandra F.; Heimburg-Molinaro, Jamie; Cummings, Richard D.; Steinhauer, David A.

doi:10.1128/jvi.01178-19

Cited by 37 publications

(45 citation statements)

References 31 publications

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“…Several 2,3-and 2,6-sialylated biantennary N-glycans were identified to be positively bound by influenza strains, which was an exciting development for studying endogenous glycan ligands. This led to the broad screening of various strains of influenza viruses, including these H3N2 strains that have progressively undergone "antigenic drift" in their head domains (Byrd-Leotis et al, 2019a) Surprisingly, the H3N2 drift strains almost completely lost their capacity in binding of canonical sialylated N-glycans on the sequence-defined N-glycan array (Byrd-Leotis et al, 2019a). Moreover, the discoveries with the pig lung glycan array opened the door to later studies with actual human lung tissue to search for endogenous receptors for influenza viruses (Byrd-Leotis et al, 2019b).…”

Section: Discovery Of Natural Glycan Ligands Involved In Infection Anmentioning

confidence: 99%

Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins

et al. 2019

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Glycans and glycan binding proteins (GBPs or lectins) are essential components in almost every aspect of immunology. Investigations of the interactions between glycans and GBPs have greatly advanced our understanding of the molecular basis of these fundamental immunological processes. In order to better study the glycan-GBP interactions, microscope glass slide-based glycan microarrays were conceived and proved to be an incredibly useful and successful tool. A variety of methods have been developed to better present the glycans so that they mimic natural presentations. Breakthroughs in chemical biology approaches have also made available glycans with sophisticated structures that were considered practically impossible just a few decade ago. Glycan microarrays provide a wealth of valuable information in immunological studies. They allow for discovery of detailed glycan binding preferences or novel binding epitopes of known endogenous immune receptors, which can potentially lead to the discovery of natural ligands that carry the glycans. Glycan microarrays also serve as a platform to discover new GBPs that are vital to the process of infection and invasion by microorganisms. This review summarizes the construction strategies and the immunological applications of glycan microarrays, particularly focused on those with the most comprehensive sets of glycan structures. We also review new methods and technologies that have evolved. We believe that glycan microarrays will continue to benefit the growing research community with various interests in the field of immunology.

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Section: Discovery Of Natural Glycan Ligands Involved In Infection Anmentioning

confidence: 99%

Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins

et al. 2019

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“…For example, the inhibition of human anti-N9 antibodies to influenza neuraminidases was analyzed by glycan array [ 70 ]. The binding study of the H3N2 influenza viruses using glycan microarrays demonstrated the changes in virus hemagglutinin that affect the receptor binding properties of the viruses [ 71 ].…”

Section: Elucidation Of the Molecular Basis Of N mentioning

confidence: 99%

Recent Advances in the Chemical Biology of N-Glycans

2021

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Asparagine-linked N-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of N-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis. This has allowed for progress in the elucidation of N-glycan functions at the molecular level. Interaction analyses with lectins by glycan arrays or nuclear magnetic resonance (NMR) using various N-glycans have revealed the molecular basis for the recognition of complex structures of N-glycans. Preparation of proteins modified with homogeneous N-glycans revealed the influence of N-glycan modifications on protein functions. Furthermore, N-glycans have potential applications in drug development. This review discusses recent advances in the chemical biology of N-glycans.

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“…As synthetic arrays printed with synthetic, well‐defined glycans came into use, it became clear that not only the SA linkage, but also the structural attributes of the underlying glycan are important (Ji et al, 2017; Stencel‐Baerenwald et al, 2014). Many of these studies were performed with the Center for Disease Control (CDC) or Consortium for Functional Glycomics (CFG) (Amonsen et al, 2007; Bradley et al, 2011; Tappert, Smith, & Air, 2011; Gulati et al, 2013, 2014; Walther et al, 2013; Jernigan & Cox, 2015; Pappas et al, 2015; Pulit‐Penaloza et al, 2017; Hosoda et al, 2018; Byrd‐Leotis et al, 2019a) arrays. Detection of binding on arrays has been through direct labeling with fluorophore or through secondary detection with labeled antibody.…”

Section: Revealing the Host Side Of Viral Glycomicsmentioning

confidence: 99%

“…Natural glycan arrays, also known as shotgun arrays, have been constructed from host tissues including swine (Byrd‐Leotis et al, 2014) and human (Byrd‐Leotis et al, 2019a). If collected in sufficient quantities, fractions containing glycans of interest can be revisited and analyzed in more depth.…”

Section: Revealing the Host Side Of Viral Glycomicsmentioning

confidence: 99%

Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure–function relationships

Cipollo

Parsons

2020

Mass Spectrometry Reviews

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The advancement of viral glycomics has paralleled that of the mass spectrometry glycomics toolbox. In some regard the glycoproteins studied have provided the impetus for this advancement. Viral proteins are often highly glycosylated, especially those targeted by the host immune system. Glycosylation tends to be dynamic over time as viruses propagate in host populations leading to increased number of and/or “movement” of glycosylation sites in response to the immune system and other pressures. This relationship can lead to highly glycosylated, difficult to analyze glycoproteins that challenge the capabilities of modern mass spectrometry. In this review, we briefly discuss five general areas where glycosylation is important in the viral niche and how mass spectrometry has been used to reveal key information regarding structure–function relationships between viral glycoproteins and host cells. We describe the recent past and current glycomics toolbox used in these analyses and give examples of how the requirement to analyze these complex glycoproteins has provided the incentive for some advances seen in glycomics mass spectrometry. A general overview of viral glycomics, special cases, mass spectrometry methods and work‐flows, informatics and complementary chemical techniques currently used are discussed. © 2020 The Authors. Mass Spectrometry Reviews published by John Wiley & Sons Ltd. Mass Spec Rev

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Antigenic Pressure on H3N2 Influenza Virus Drift Strains Imposes Constraints on Binding to Sialylated Receptors but Not Phosphorylated Glycans

Cited by 37 publications

References 31 publications

Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins

Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins

Recent Advances in the Chemical Biology of N-Glycans

Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure–function relationships

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