Sialic acid profiles in the respiratory tracts of selected species of raptors: evidence for potential binding sites for human and avian influenza A viruses

Context The ability of influenza A viruses to recognise and bind to cell surface receptors such as sialic acid linked to galactose by an α2,3 linkage (SAα2,3-gal) and sialic acid linked to galactose by an α2,6 linkage (SAα2,6-gal) is a major determinant of influenza A virus infection. Although the epidemiological surveys of influenza A virus infection in raptors suggest that some raptor species are susceptible to influenza A viruses under natural conditions, the sialic acid profiles in the respiratory and intestinal tracts of raptors are unknown. Aims To examine the sialic acid receptor profiles in the respiratory tracts of the selected raptor species and assess the potential susceptibility of raptors to avian and human influenza viruses and the role of raptors in the epidemiology and evolution of influenza A viruses. Methods The lectin immunohistochemistry staining method was used to examine the sialic acid profiles in the respiratory tracts of eight different species of raptors. Key results A strong staining with Maackia amurensis agglutinin (MAA), specific for sialic acid linked to galactose by an α2,3 linkage (SAα2,3-gal), was observed in the epithelial cells of the respiratory tract of Accipiter nisus and Falco tinnunculus. However, a positive staining for both MAA and Sambucus nigra agglutinin (SNA), specific for sialic acid linked to galactose by an α2,6 linkage (SAα2,6-gal), was detected in the epithelial cells of the upper respiratory tract of Accipiter gularis, Buteo buteo, Otus sunia, Bubo bubo and Asio otus, and in the epithelial cells of the alveoli of Buteo buteo, Falco peregrinus, Otus sunia and Bubo bubo. Conclusions Both avian and human influenza A virus receptors are expressed in six species of raptors examined. There are some variations in the type and distribution of sialic acid receptor expression among different raptor species. No correlation between phylogeny of birds and their sialic acid receptor distributions was observed. Implications Since SAα2,3-gal and SAα2,6-gal are often considered as the primary receptors for avian influenza A viruses and human influenza A viruses, respectively, our data suggest that raptors could be a potential host for avian and human influenza A viruses.

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Identification of sequence mutations affecting hemagglutinin specificity to sialic acid receptor in influenza A virus subtypes

Bioinformation ◽

10.6026/97320630005244 ◽

2010 ◽

Vol 5 (6) ◽

pp. 244-249 ◽

Cited By ~ 7

Author(s):

Usman Sumo Friend Tambunan ◽

Ramdhan

Keyword(s):

Sialic Acid ◽

Influenza A Virus ◽

Influenza A ◽

Acid Receptor ◽

Sialic Acid Receptor

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N-Glycolylneuraminic Acid in Animal Models for Human Influenza A Virus

Viruses ◽

10.3390/v13050815 ◽

2021 ◽

Vol 13 (5) ◽

pp. 815

Author(s):

Cindy M. Spruit ◽

Nikoloz Nemanichvili ◽

Masatoshi Okamatsu ◽

Hiromu Takematsu ◽

Geert-Jan Boons ◽

...

Keyword(s):

Sialic Acid ◽

Animal Models ◽

Influenza A ◽

Influenza Virus Infection ◽

Influenza Viruses ◽

Upper Respiratory Tract ◽

Human Influenza ◽

Influenza A Viruses ◽

Sialic Acid Content ◽

Acetylneuraminic Acid

The first step in influenza virus infection is the binding of hemagglutinin to sialic acid-containing glycans present on the cell surface. Over 50 different sialic acid modifications are known, of which N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc) are the two main species. Animal models with α2,6 linked Neu5Ac in the upper respiratory tract, similar to humans, are preferred to enable and mimic infection with unadapted human influenza A viruses. Animal models that are currently most often used to study human influenza are mice and ferrets. Additionally, guinea pigs, cotton rats, Syrian hamsters, tree shrews, domestic swine, and non-human primates (macaques and marmosets) are discussed. The presence of NeuGc and the distribution of sialic acid linkages in the most commonly used models is summarized and experimentally determined. We also evaluated the role of Neu5Gc in infection using Neu5Gc binding viruses and cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMAH)-/- knockout mice, which lack Neu5Gc and concluded that Neu5Gc is unlikely to be a decoy receptor. This article provides a base for choosing an appropriate animal model. Although mice are one of the most favored models, they are hardly naturally susceptible to infection with human influenza viruses, possibly because they express mainly α2,3 linked sialic acids with both Neu5Ac and Neu5Gc modifications. We suggest using ferrets, which resemble humans closely in the sialic acid content, both in the linkages and the lack of Neu5Gc, lung organization, susceptibility, and disease pathogenesis.

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Upregulation of cell-surface mucin MUC15 in human nasal epithelial cells upon influenza A virus infection

BMC Infectious Diseases ◽

10.1186/s12879-019-4213-y ◽

2019 ◽

Vol 19 (1) ◽

Cited By ~ 3

Author(s):

Zhuang Gui Chen ◽

Zhao Ni Wang ◽

Yan Yan ◽

Jing Liu ◽

Ting Ting He ◽

...

Keyword(s):

Epithelial Cells ◽

Virus Infection ◽

Cell Surface ◽

Influenza A Virus ◽

Influenza A ◽

Nasal Epithelial Cells ◽

Human Nasal Epithelial Cells ◽

Influenza A Virus Infection

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Cooperation between the Hemagglutinin of Avian Viruses and the Matrix Protein of Human Influenza A Viruses

Journal of Virology ◽

10.1128/jvi.76.4.1781-1786.2002 ◽

2002 ◽

Vol 76 (4) ◽

pp. 1781-1786 ◽

Cited By ~ 40

Author(s):

Christoph Scholtissek ◽

Jürgen Stech ◽

Scott Krauss ◽

Robert G. Webster

Keyword(s):

Influenza A Virus ◽

Influenza A ◽

Matrix Protein ◽

Gene Products ◽

Human Influenza ◽

Influenza A Viruses ◽

M Gene ◽

Human Virus ◽

Ha Gene ◽

M Proteins

ABSTRACT To analyze the compatibility of avian influenza A virus hemagglutinins (HAs) and human influenza A virus matrix (M) proteins M1 and M2, we doubly infected Madin-Darby canine kidney cells with amantadine (1-aminoadamantane hydrochloride)-resistant human viruses and amantadine-sensitive avian strains. By using antisera against the human virus HAs and amantadine, we selected reassortants containing the human virus M gene and the avian virus HA gene. In our system, high virus yields and large, well-defined plaques indicated that the avian HAs and the human M gene products could cooperate effectively; low virus yields and small, turbid plaques indicated that cooperation was poor. The M gene products are among the primary components that determine the species specificities of influenza A viruses. Therefore, our system also indicated whether the avian HA genes effectively reassorted into the genome and replaced the HA gene of the prevailing human influenza A viruses. Most of the avian HAs that we tested efficiently cooperated with the M gene products of the early human A/PR/8/34 (H1N1) virus; however, the avian HAs did not effectively cooperate with the most recently isolated human virus that we tested, A/Nanchang/933/95 (H3N2). Cooperation between the avian HAs and the M proteins of the human A/Singapore/57 (H2N2) virus was moderate. These results suggest that the currently prevailing human influenza A viruses might have lost their ability to undergo antigenic shift and therefore are unable to form new pandemic viruses that contain an avian HA, a finding that is of great interest for pandemic planning.

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