Evolving complexities of influenza virus and its receptors

Nicholls, John M.; Chan, Wing-Yee; Russell, Rosemary; Air, Gillian M.; Peiris, Malik

doi:10.1016/j.tim.2008.01.008

Cited by 193 publications

(210 citation statements)

References 73 publications

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“…Glycan 20, which is an ␣2-6 monosialylated derivative of NA2, bound RCA-I before and after neuraminidase, although binding was not enhanced after neuraminidase treatment. RCA-I bound weakly to ␣2-6-sialylated lactose and LNnT (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17), unlike the corresponding ␣2-3-sialylated lactose and LNnT (41-57), which were not bound. Although most sialic acid derivatives moderately decreased RCA-I binding to NA2, ␣2-6-sialylation with Neu5Ac8Me (19) and Neu5Gc9Ac (25) greatly inhibit RCA-I binding.…”

Section: Resultsmentioning

confidence: 99%

“…The Binding of Viruses to the SGM-Influenza viruses bind sialic acid on cell surfaces via hemagglutinin, and their specificities toward ␣6-linked sialic acid and ␣3-linked sialic acid are associated with their ability to infect humans or birds, respectively (6). Their specificities for the various modifications of sialic acid, however, have not been systematically studied due to the lack of available glycans.…”

Section: Resultsmentioning

confidence: 99%

“…Here we have described screening assays using several samples of viruses that are known or suspected to bind to sialylated glycans. During the initiation of infection, many viruses, such as influenza A, bind to cell surface sialic acids (6,8). Although significant data have accumulated that correlate virus binding specificities directed at ␣2-3-or ␣2-6-linked sialic acid with infection of avian and human populations, respectively, most studies have focused attention on differences in the underlying glycans.…”

Section: Discussionmentioning

confidence: 99%

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A Sialylated Glycan Microarray Reveals Novel Interactions of Modified Sialic Acids with Proteins and Viruses

Song

Chen

et al. 2011

Journal of Biological Chemistry

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136

115

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Many glycan-binding proteins in animals and pathogens recognize sialic acid or its modified forms, but their molecular recognition is poorly understood. Here we describe studies on sialic acid recognition using a novel sialylated glycan microarray containing modified sialic acids presented on different glycan backbones. Glycans terminating in ␤-linked galactose at the nonreducing end and with an alkylamine-containing fluorophore at the reducing end were sialylated by a one-pot three-enzyme system to generate ␣2-3-and ␣2-6-linked sialyl glycans with 16 modified sialic acids. The resulting 77 sialyl glycans were purified and quantified, characterized by mass spectrometry, covalently printed on activated slides, and interrogated with a number of key sialic acid-binding proteins and viruses. Sialic acid recognition by the sialic acid-binding lectins Sambucus nigra agglutinin and Maackia amurensis lectin-I, which are routinely used for detecting ␣2-6-and ␣2-3-linked sialic acids, are affected by sialic acid modifications, and both lectins bind glycans terminating with 2-keto-3-deoxy-D-glycero-D-galactonononic acid (Kdn) and Kdn derivatives stronger than the derivatives of more common N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc). Three human parainfluenza viruses bind to glycans terminating with Neu5Ac or Neu5Gc and some of their derivatives but not to Kdn and its derivatives. Influenza A virus also does not bind glycans terminating in Kdn or Kdn derivatives. An especially novel aspect of human influenza A virus binding is its ability to equivalently recognize glycans terminated with either ␣2-6-linked Neu5Ac9Lt or ␣2-6-linked Neu5Ac. Our results demonstrate the utility of this sialylated glycan microarray to investigate the biological importance of modified sialic acids in protein-glycan interactions.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

A Sialylated Glycan Microarray Reveals Novel Interactions of Modified Sialic Acids with Proteins and Viruses

Song

Chen

et al. 2011

Journal of Biological Chemistry

Self Cite

136

115

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“…IAVs have an antisense RNA genome that is divided into eight segments, which allows genetic reassortment between different viruses 2. The viral surface glycoproteins hemagglutinin (HA) and neuraminidase (NA) are the main targets of the host immune response, and they are important for virulence and host specificity 3. Three subtypes of swine influenza virus (SIV) are currently circulating in the swine population globally: H1N1, H3N2, and H1N2 1…”

Section: Introductionmentioning

confidence: 99%

Genetic characterization of influenza virus circulating in Brazilian pigs during 2009 and 2010 reveals a high prevalence of the pandemic H1N1 subtype

Rajão

Costa

Brasil

et al. 2012

Influenza Resp Viruses

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BackgroundInfluenza A viruses circulating in pigs in Brazil are still not characterized, and only limited data are available about swine influenza epidemiology in the country. Therefore, we characterized the hemagglutinin (HA) and neuraminidase (NA) genes of influenza viruses isolated from Brazilian pigs. We also evaluated one case of probable swine‐to‐human transmission.MethodsTwenty influenza viruses isolated from pigs during 2009–2010 in five Brazilian states (Minas Gerais, Sao Paulo, Parana, Rio Grande do Sul, and Mato Grosso) were used. One human isolate, from a technician who became ill after visiting a swineherd going through a respiratory disease outbreak, was also used in the study. Phylogenetic analysis for the HA and NA genes and hemagglutinin amino acid sequence alignment were performed.ResultsAll isolates clustered with pandemic H1N1 2009 (pH1N1) viruses and appeared to have a common ancestor. Genetic diversity was higher in the HA than in the NA gene, and the amino acid substitution S203T in one of HA's antigenic sites was found in most of the samples. The human isolate was more related to swine isolates from the same herd visited by the technician than to other human isolates, suggesting swine‐to‐human transmission.ConclusionOur results show that pH1N1 was disseminated and the predominant subtype in Brazilian pigs in 2009–2010.

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“…In addition, the segmented genome of influenza virus facilitates "antigenic shift", a reassortment between more than one isolate when they co-infect the same host cell; a virus acquires HA of a novel subtype from the other, which generates a novel combination of HA and NA antigens to which the population is immunologically naïve [14] . Receptor preference (usage) of each virus strain can be another factor to determine the cell tropism [22] . The binding of influenza viruses to their target cells (basically epithelial cells in upper respiratory tract) is mediated by viral HA, and binding preference to specific receptors is a crucial step in influenza virus infection efficiency [22] .…”

Section: Properties Of Influenza Virusesmentioning

confidence: 99%

Swine-origin influenza-virus-induced acute lung injury: Novel or classical pathogenesis?

Maeda

Uede

2010

WJBC

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Influenza viruses are common respiratory pathogens in humans and can cause serious infection that leads to the development of pneumonia. Due to their hostrange diversity, genetic and antigenic diversity, and potential to reassort genetically in vivo , influenza A viruses are continual sources of novel influenza strains that lead to the emergence of periodic epidemics and outbreaks in humans. Thus, newly emerging viral diseases are always major threats to public health. In March 2009, a novel influenza virus suddenly emerged and caused a worldwide pandemic. The novel pandemic influenza virus was genetically and antigenically distinct from previous seasonal human influenza A/H1N1 viruses; it was identified to have originated from pigs, and further genetic analysis revealed it as a subtype of A/H1N1, thus later called a swine-origin influenza virus A/H1N1. Since the novel virus emerged, epidemiological surveys and research on experimental animal models have been conducted, and characteristics of the novel influenza virus have been determined but the exact mechanisms of pulmonary pathogenesis remain to be elucidated. In this editorial, we summarize and discuss the recent pandemic caused by the novel swine-origin influenza virus A/H1N1 with a focus on the mechanism of pathogenesis to obtain an insight into potential therapeutic strategies.

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Evolving complexities of influenza virus and its receptors

Cited by 193 publications

References 73 publications

A Sialylated Glycan Microarray Reveals Novel Interactions of Modified Sialic Acids with Proteins and Viruses

A Sialylated Glycan Microarray Reveals Novel Interactions of Modified Sialic Acids with Proteins and Viruses

Genetic characterization of influenza virus circulating in Brazilian pigs during 2009 and 2010 reveals a high prevalence of the pandemic H1N1 subtype

Swine-origin influenza-virus-induced acute lung injury: Novel or classical pathogenesis?

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