N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity

Hausmann, Jürgen; Kretzschmar, Evelyne; Garten, Wolfgang; Klenk, Hans‐Dieter

doi:10.1099/0022-1317-76-7-1719

Cited by 40 publications

(47 citation statements)

References 24 publications

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“…This site bears no resemblance to either the NA active site or the HA sialic acid binding site, and indeed the specificity of binding is unlike that of HA, in that the bound sialic acid is not released by N9 or N2 NA activity but only by bacterial sialidases of very broad specificity 60 . HB activity was also found in the N1 NA of fowl plague virus 61 . Comparisons of sequences in the area of the second binding site suggested that avian viruses have the HB activity while human viruses do not 59,61,62 , but so far a specific function of the HB activity in bird viruses has not been established.…”

Section: Some Nas Have a Second Sialic Acid Binding Sitementioning

confidence: 87%

Influenza neuraminidase

Air

2011

Influenza Resp Viruses

215

216

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Influenza neuraminidase is the target of two licensed antivirals that have been very successful, with several more in development. However, neuraminidase has been largely ignored as a vaccine target despite evidence that inclusion of neuraminidase in the subunit vaccine gives increased protection. This article describes current knowledge on the structure, enzyme activity and antigenic significance of neuraminidase.

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Section: Some Nas Have a Second Sialic Acid Binding Sitementioning

confidence: 87%

Influenza neuraminidase

Air

2011

Influenza Resp Viruses

215

216

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“…Another potential role of NA was suggested in that it may permit transport of the virus through the mucin layer present in the respiratory tract, facilitating the virus interaction with the target epithelial cells. Some NA (N1 and N9 subtypes) have both a receptor-binding site and a NA active site [43,44]. However, the receptor speci®city and function of this receptor-binding activity is still unknown.…”

Section: Discussionmentioning

confidence: 99%

Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses

Lin¹,

Chouljenko²,

Kousoulas³

et al. 2000

Journal of Medical Microbiology

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Numerous respiratory bovine coronaviruses (RBCV) were isolated recently from nasal swab samples and lung tissues of feedlot cattle with acute respiratory tract disease. These newly emerging RBCV isolates exhibited distinct phenotypic features that differentiated them from enteropathogenic bovine coronaviruses (EBCV). The RBCV strains had a receptor-destroying enzyme function mediated by acetylesterase (AE) activity of the haemagglutinin-esterase (HE) glycoprotein. The HE genes of wild-type EBCV strain LY138 and RBCV strains OK-0514 (OK) and LSU-94LSS-051 (LSU) were cloned, sequenced and transiently expressed in COS-7 cells. The enzymic properties of HE proteins in COS-7 cellular extracts and in puri®ed virus preparations were assayed at room temperature, 378C and 398C by two different assays. One assay used r rnitrophenyl acetate (PNPA) as substrate and detected serine-esterase activity; the second assay monitored AE function with bovine submaxillary mucin (BSM) as substrate. The PNPA tests con®rmed that HE proteins of EBCV and RBCV were functionally expressed in transfected COS-7 cells. Time-dependent determination of the AE activity of puri®ed RBCV OK and LSU particles showed lower AE activity at 398C than at 378C, whereas the puri®ed EBCV LY particles retained full AE activity at both 378C and 398C. Transiently expressed RBCV HE exhibited a marked reduction of AE activity after 40 min of assay time at 378C. In contrast, the AE activity of the transiently expressed EBCV HE remained stable beyond 40 min. The deduced amino-acid sequences of the HE proteins speci®ed by the RBCV strains OK and LSU contained speci®c amino-acid changes in comparison with the EBCV LY strain, which may be responsible for the observed enzymic differences. These results are consistent with the hypothesis that RBCV strains have evolved to selectively replicate in respiratory tissues and that HE may play a role in this tissue tropism.

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“…However, residue 151, unlike residue 150, is categorized as a catalytic site residue and is believed to stabilize the transition state intermediate [26]. The position of these residues in or close to the catalytic site and the inhibition of NAmediated binding by oseltamivir suggest that the binding of NA to turkey erythrocytes is mediated via the catalytic site and not via haemadsorption sites, which are secondary sialic acid-binding sites that have been described for some avian NAs [27][28][29][30][31]. At the moment it is not clear what mechanism is involved in the 150HR-mediated binding of erythrocytes and what functional changes are caused in NA by this amino acid substitution.…”

Section: Discussionmentioning

confidence: 99%

Neuraminidase-mediated haemagglutination of recent human influenza A(H3N2) viruses is determined by arginine 150 flanking the neuraminidase catalytic site

Mögling

Richard

Vliet

et al. 2017

Journal of General Virology

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Over the last decade, an increasing proportion of circulating human influenza A(H3N2) viruses exhibited haemagglutination activity that was sensitive to neuraminidase inhibitors. This change in haemagglutination as compared to older circulating A(H3N2) viruses prompted an investigation of the underlying molecular basis. Recent human influenza A(H3N2) viruses were found to agglutinate turkey erythrocytes in a manner that could be blocked with either oseltamivir or neuraminidase-specific antisera, indicating that agglutination was driven by neuraminidase, with a low or negligible contribution of haemagglutinin. Using representative virus recombinants it was shown that the haemagglutinin of a recent A(H3N2) virus indeed had decreased activity to agglutinate turkey erythrocytes, while its neuraminidase displayed increased haemagglutinating activity. Viruses with chimeric and mutant neuraminidases were used to identify the amino acid substitution histidine to arginine at position 150 flanking the neuraminidase catalytic site as the determinant of this neuraminidase-mediated haemagglutination. An analysis of publicly available neuraminidase gene sequences showed that viruses with histidine at position 150 were rapidly replaced by viruses with arginine at this position between 2005 and 2008, in agreement with the phenotypic data. As a consequence of neuraminidase-mediated haemagglutination of recent A(H3N2) viruses and poor haemagglutination via haemagglutinin, haemagglutination inhibition assays with A(H3N2) antisera are no longer useful to characterize the antigenic properties of the haemagglutinin of these viruses for vaccine strain selection purposes. Continuous monitoring of the evolution of these viruses and potential consequences for vaccine strain selection remains important.

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N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity

Cited by 40 publications

References 24 publications

Influenza neuraminidase

Influenza neuraminidase

Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses

Neuraminidase-mediated haemagglutination of recent human influenza A(H3N2) viruses is determined by arginine 150 flanking the neuraminidase catalytic site

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