scholarly journals Influenza D virus diverges from its related influenza C virus in the recognition of 9-O-acetylated N-acetyl- or N-glycolyl-neuraminic acid-containing glycan receptors

Virology ◽  
2020 ◽  
Vol 545 ◽  
pp. 16-23 ◽  
Author(s):  
Runxia Liu ◽  
Chithra Sreenivasan ◽  
Hai Yu ◽  
Zizhang Sheng ◽  
Simon J. Newkirk ◽  
...  
Keyword(s):  
Neuraminic Acid ◽  
Influenza C Virus ◽  
Glycan Receptors

Neuraminic acid is involved in the binding of influenza C virus to erythrocytes

Virology ◽  
1985 ◽  
Vol 141 (1) ◽  
pp. 144-147 ◽  
Author(s):  
G. Herrler ◽  
R. Rott ◽  
H.-D. Klenk
Keyword(s):  
Neuraminic Acid ◽  
Influenza C Virus

scholarly journals Infectious Salmon Anemia Virus Specifically Binds to and Hydrolyzes 4-O-Acetylated Sialic Acids

2004 ◽  
Vol 78 (6) ◽  
pp. 3055-3062 ◽  
Author(s):  
Audny Hellebø ◽  
Ulrike Vilas ◽  
Knut Falk ◽  
Reinhard Vlasak
Keyword(s):  
Sialic Acid ◽  
Sialic Acids ◽  
Neuraminic Acid ◽  
Infectious Salmon Anemia Virus ◽  
Infectious Salmon Anemia ◽  
Influenza C Virus ◽  
Salmon Anemia Virus ◽  
Group 2 ◽  
Farmed Atlantic Salmon ◽  
Anemia Virus

ABSTRACT Infectious salmon anemia virus (ISAV) is the causative agent of infections in farmed Atlantic salmon. ISAV presumably represents a new genus within the Orthomyxoviridae. ISAV has been shown earlier to exhibit a receptor-destroying activity, which was defined as an acetylesterase with unknown specificity. We have analyzed the substrate specificity of the ISAV esterase in detail. Purified ISAV hydrolyzed free 5-N-acetyl-4-O-acetyl neuraminic acid. In addition, the purified 9-O-acetylated sialic acid derivative was also hydrolyzed, but at lower rates. When we used a glycosidically bound substrate, ISAV was unable to hydrolyze 9-O-acetylated sialic acid, which represents the major substrate for the influenza C virus esterase. ISAV completely de-O-acetylated glycoprotein-bound 5-N-acetyl-4-O-acetyl neuraminic acid. Thus, the enzymatic activity of the hemagglutinin-esterase of ISAV is comparable to that of the sialate-4-O-esterases of murine coronaviruses and related group 2 coronaviruses. In addition, we found that ISAV specifically binds to glycoproteins containing 4-O-acetylated sialic acids. Both the ISAV esterase and recombinant rat coronavirus esterase specific for 4-O-acetylated sialic acids hydrolyzed ISAV receptors on horse and rabbit erythrocytes, indicating that this sialic acid represents a receptor determinant for ISAV.

CHEMISTRY OF GONADOTROPHINS IN RELATION TO THEIR ANTIGENIC PROPERTIES

1969 ◽  
Vol 62 (1_Suppl) ◽  
pp. S13-S30 ◽  
Author(s):  
W. R. Butt
Keyword(s):  
Biological Activity ◽  
Guinea Pigs ◽  
Complement Fixation ◽  
Neuraminic Acid ◽  
Fixation Technique ◽  
Immunological Activity ◽  
Antigenic Properties ◽  
Specific Antisera ◽  
Structural Differences

ABSTRACT Several chemical differences between FSH, LH and HCG have been reported: thus LH and HCG are richer in proline than FSH and FSH and HCG contain more N-acetyl neuraminic acid than LH. Sub-units of LH are formed by treatment with urea, guanidine or acid. HCG also may contain two sub-units. The sub-units from LH are biologically inert but retain their immunological activity: biological activity is restored when the sub-units are incubated together. There is much evidence from chemical and enzymic reactions that antigenic groups are distinct from those parts of the molecule essential for biological activity. N-acetyl neuraminic acid and probably other carbohydrates in FSH and HCG are not involved in immunological activity but are necessary for biological activity. Histidine, methionine and possibly cysteine appear to be essential for biological but not immunological activity of FSH, while tryptophan and possibly tyrosine are not essential for either. A few highly specific antisera to gonadotrophins have been prepared in rabbits and guinea pigs to crude antigens: there is no evidence that purified antigens are more likely to produce specific antisera. Differences in the immunological reactivities of urinary compared with pituitary gonadotrophins have been observed both by radioimmunoassay and by the complement fixation technique. The latter may be particularly useful for detecting structural differences in the hormones.

Identification of a Coronavirus Hemagglutinin-Esterase with a Substrate Specificity Different from Those of Influenza C Virus and Bovine Coronavirus

1999 ◽  
Vol 73 (5) ◽  
pp. 3737-3743 ◽  
Author(s):  
Alfred Klausegger ◽  
Birgit Strobl ◽  
Gerhard Regl ◽  
Alexandra Kaser ◽  
Willem Luytjes ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Solid Phase ◽  
Hepatitis Virus ◽  
Bovine Brain ◽  
Brain Extract ◽  
Binding Assays ◽  
Bovine Coronavirus ◽  
Close Relationship ◽  
Influenza C Virus ◽  
Cloned Gene

ABSTRACT We have characterized the hemagglutinin-esterase (HE) of puffinosis virus (PV), a coronavirus closely related to mouse hepatitis virus (MHV). Analysis of the cloned gene revealed approximately 85% sequence identity to HE proteins of MHV and approximately 60% identity to the corresponding esterase of bovine coronavirus. The HE protein exhibited acetylesterase activity with synthetic substratesp-nitrophenyl acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate. In contrast to other viral esterases, no activity was detectable with natural substrates containing 9-O-acetylated sialic acids. Furthermore, PV esterase was unable to remove influenza C virus receptors from human erythrocytes, indicating a substrate specificity different from HEs of influenza C virus and bovine coronavirus. Solid-phase binding assays revealed that purified PV was unable to bind to sialic acid-containing glycoconjugates like bovine submaxillary mucin, mouse α1macroglobulin or bovine brain extract. Because of the close relationship to MHV, possible implications on the substrate specificity of MHV esterases are suggested.

scholarly journals Prevalence of BRD-Related Viral Pathogens in the Upper Respiratory Tract of Swiss Veal Calves

Animals ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1940
Author(s):  
Eveline Studer ◽  
Lutz Schönecker ◽  
Mireille Meylan ◽  
Dimitri Stucki ◽  
Ronald Dijkman ◽  
...  
Keyword(s):  
Risk Factors ◽  
Welfare Economic ◽  
Economic Losses ◽  
Nasopharyngeal Swab ◽  
Upper Respiratory Tract ◽  
Convenience Sample ◽  
Veal Calves ◽  
Mixed Regression ◽  
Influenza C Virus ◽  
Syncytial Virus

The prevention of bovine respiratory disease is important, as it may lead to impaired welfare, economic losses, and considerable antimicrobial use, which can be associated with antimicrobial resistance. The aim of this study was to describe the prevalence of respiratory viruses and to identify risk factors for their occurrence. A convenience sample of 764 deep nasopharyngeal swab samples from veal calves was screened by PCR for bovine respiratory syncytial virus (BRSV), bovine parainfluenza-3 virus (BPI3V), bovine coronavirus (BCoV), influenza D virus (IDV), and influenza C virus (ICV). The following prevalence rates were observed: BRSV, 2.1%; BPI3V, 3.3%; BCoV, 53.5%; IDV, 4.1%; ICV, 0%. Logistic mixed regression models were built for BCoV to explore associations with calf management and housing. Positive swab samples were more frequent in younger calves than older calves (>100 days; p < 0.001). The probability of detecting BCoV increased with increasing group size in young calves. Findings from this study suggested that young calves should be fattened in small groups to limit the risk of occurrence of BCoV, although an extended spectrum of risk factors for viral associated respiratory disorders such as nutritional aspects should be considered in future studies.

scholarly journals In situ structure and organization of the influenza C virus surface glycoprotein

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Steinar Halldorsson ◽  
Kasim Sader ◽  
Jack Turner ◽  
Lesley J. Calder ◽  
Peter B. Rosenthal
Keyword(s):  
Membrane Fusion ◽  
Hexagonal Lattice ◽  
Surface Glycoprotein ◽  
Structural Basis ◽  
Virus Surface ◽  
The Matrix ◽  
Influenza C Virus ◽  
Subtomogram Averaging ◽  
Electron Cryotomography

AbstractThe lipid-enveloped influenza C virus contains a single surface glycoprotein, the haemagglutinin-esterase-fusion (HEF) protein, that mediates receptor binding, receptor destruction, and membrane fusion at the low pH of the endosome. Here we apply electron cryotomography and subtomogram averaging to describe the structural basis for hexagonal lattice formation by HEF on the viral surface. The conformation of the glycoprotein in situ is distinct from the structure of the isolated trimeric ectodomain, showing that a splaying of the membrane distal domains is required to mediate contacts that form the lattice. The splaying of these domains is also coupled to changes in the structure of the stem region which is involved in membrane fusion, thereby linking HEF’s membrane fusion conformation with its assembly on the virus surface. The glycoprotein lattice can form independent of other virion components but we show a major role for the matrix layer in particle formation.

Studies on the Biosynthesis of Neuraminic Acid

Nature ◽  
1956 ◽  
Vol 178 (4539) ◽  
pp. 917-918 ◽  
Author(s):  
KARL LAUENSTEIN ◽  
KURT I. ALTMAN
Keyword(s):  
Neuraminic Acid

scholarly journals Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes

2005 ◽  
Vol 86 (5) ◽  
pp. 1455-1465 ◽  
Author(s):  
Andrea Hanika ◽  
Birthe Larisch ◽  
Eike Steinmann ◽  
Christel Schwegmann-Weßels ◽  
Georg Herrler ◽  
...  
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Receptor Binding ◽  
Viral Vectors ◽  
Basolateral Membrane ◽  
Apical Plasma Membrane ◽  
Pseudotyped Virus ◽  
Proteolytic Activation ◽  
Multifunctional Protein ◽  
Influenza C Virus ◽  
Vesicular Stomatitis

Influenza C virus contains two envelope glycoproteins: CM2, a putative ion channel protein; and HEF, a unique multifunctional protein that performs receptor-binding, receptor-destroying and fusion activities. Here, it is demonstrated that expression of HEF is sufficient to pseudotype replication-incompetent vesicular stomatitis virus (VSV) that lacks the VSV glycoprotein (G) gene. The pseudotyped virus showed characteristic features of influenza C virus with respect to proteolytic activation, receptor usage and cell tropism. Chimeric glycoproteins composed of HEF ectodomain and VSV-G C-terminal domains were efficiently incorporated into VSV particles and showed receptor-binding and receptor-destroying activities but, unlike authentic HEF, did not mediate efficient infection, probably because of impaired fusion activity. HEF-pseudotyped VSV efficiently infected polarized Madin–Darby canine kidney cells via the apical plasma membrane, whereas entry of VSV-G-complemented virus was restricted to the basolateral membrane. These findings suggest that pseudotyping of viral vectors with HEF might be useful for efficient apical gene transfer into polarized epithelial cells and for targeting cells that express 9-O-acetylated sialic acids.

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