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PubMed2000

Integrin alpha2beta1 mediates the cell attachment of the rotavirus neuraminidase-resistant variant nar3.

It was previously reported that integrins alpha2beta1, alpha4beta1, and alphaXbeta2 are involved in rotavirus cell infection. In this work we studied the role of integrin subunits alpha2, alpha4, and beta2 on the attachment of rotaviruses RRV and nar3 to MA104 cells. Integrin alpha2beta1 was found to serve as the binding receptor for the neuraminidase-resistant virus nar3, whereas the neuraminidase-sensitive strain RRV interacted with this integrin at a postattachment step. It was shown that nar3 binds alpha2beta1 through the DGE integrin-recognition motif located in the virus surface protein VP5. Integrin subunits alpha4 and beta2 do not seem to be involved in the initial cell binding of either virus.

Antibodies, Monoclonal↗
PubMed2001

Neuraminidase from a bacterial source enhances both HIV-1-mediated syncytium formation and the virus binding/entry process.

Neuraminidases, also termed sialidases, which catalyze the removal of sialic acid residues from various glycoconjugates, have been previously reported to modulate HIV-1 replication. Given that some of the known opportunistic microbes found in patients infected with HIV-1 harbor neuraminidase (NA) activity, we speculated that pathogen-derived NA might be envisaged as an important factor in the pathogenesis of this retroviral infection. In the present study, we have monitored the putative modulation of HIV-1-mediated syncytium formation and virus replication by highly purified bacterial-derived NA from Arthrobacter ureafaciens. Taking advantage of a luciferase-based syncytium quantitative assay, we demonstrate here that the level of HIV-1-mediated syncytium formation is enhanced in the presence of NA and that it necessitates interaction between gp120 and CD4/chemokine coreceptor. By using pseudotyped recombinant luciferase-encoding HIV-1 particles, we found that NA treatment of human CD4-positive target cells (i.e., T lymphoid, monocytoid, and peripheral blood mononuclear cells) significantly augmented single-round infection by T- and macrophage-tropic isolates of HIV-1. The observed increase in HIV-1 infection was linked with an enhancement in the initial steps of the virus replicative cycle as monitored by viral binding and entry assays. Interestingly, NA treatment also enhances infectivity of HIV-1 pseudotypes with envelope glycoprotein from the amphotropic murine leukemia virus or the vesicular stomatitis virus. Taken together, our results provide useful information regarding the possible contribution of microbial agents carrying NA activity to HIV-1 pathogenesis.

Arthrobacter↗
PubMed1979

A case of neuraminidase deficiency associated with a partial beta-galactosidase defect. Clinical, biochemical and radiological studies.

Neuraminidase deficiency towards fetuin, 2 leads to 3 sialyllactose and 2 leads to 6 sialyllactose was found in cultured skin fibroblasts from a 10-year-old Japanese girl who exhibits craniofacial dysmorphism, a short neck, vertebral and pelvic deformities and macular cherry-red spots. Neuraminidase deficiency in this case seems the primary enzyme defect because the enzyme activity of her parents was intermediate. In addition, beta-galactosidase in leukocytes and cultured skin fibroblasts from the patient was found to be severely deficient, but could be detected in serum and urine. In the parents, beta-galactosidase activity was normal. There were moderately increased levels of urinary sialic acid-rich oligosaccharides and glycopeptides in the patient. The clinical and biochemical observations suggest that this case is very close to mucolipidosis I.

Cells, Cultured↗
PubMed1986

Antigenic relationships between avian paramyxoviruses. I. Quantitative characteristics based on hemagglutination and neuraminidase inhibition tests.

Comprehensive hemagglutination inhibition (HI) and neuraminidase inhibition (NI) cross reaction tests were performed using 8 of 9 serotypes of avian paramyxoviruses (PMV). The studies were designed as full scale repeating experiments which permitted an adequate statistical treatment and elaboration of quantitative criteria of antigenic kinship. The results have shown diverse antigenic relationships between different avian paramyxovirus (PMV) serotypes which were asymmetric in some cases. The antigenic relationships found by HI test did not always parallel those found by NI tests. The antigenic inter-relationships have been displayed quantitatively in a diagram. This has given a basis for some suggestions concerning: the independent antigenic drift of the HA and Nase antigenic sites of hemagglutinin-neuraminidase (HN) glycoprotein of avian PMVs; a tentative subdivision of the whole group of avian PMVs into two subgroups: the first including PMV-2 and PMV-6 serotypes and the second including PMV-1, PMV-3, PMV-4, PMV-7, PMV-8 and PMV-9 serotypes; the conception that genomic material coding for the HN glycoprotein consists of a "common-to-all-the-PMVs" portion and a "serotype-specific" portion, on one hand, and of a "conserved" portion and a "variable" portion, on the other; the ratios between the portions have been shown to be different for, at least, certain PMV serotypes; the evolutionary pathways of the avain PMV HN antigenic drift.

Animals↗
PubMed1994

Rapid detection of influenza A neuraminidase subtypes by cDNA amplification coupled to a simple DNA enzyme immunoassay.

A newly developed colorimetric method, DNA enzyme immunoassay (DEIA), was applied to the detection of neuraminidase subtypes N1 and N2 of influenza A viruses. Reverse transcription and polymerase chain reaction with universal primers were used for genomic amplification of H1N1, H2N2, and H3N2 strains. Following amplification, an aliquot of the PCR product was hybridized to biotinylated DNA sequences (N1/N2 probes) immobilized on microtiter wells. The hybridization event was revealed by monoclonal antibodies to double stranded DNA in a standard ELISA reaction. The assay described here was able to distinguish accurately between the two neuraminidase subtypes of human influenza A viruses. It is a simple and rapid method facilitating the handling of a large number of samples and therefore seems to be easily applicable to diagnostic laboratories.

Base Sequence↗
PubMed1988

Complete nucleotide sequence of the neuraminidase gene of the human influenza virus A/Chile/1/83 (H1N1). Brief report.

The complete nucleotide sequence of the neuraminidase (NA) gene of influenza virus A/Chile/1/83 (H1N1) has been determined after reverse transcription and cloning into the plasmid pAT 153/PvuII/8. The gene is 1461 nucleotides long and codes for a protein of 470 amino acids. The overall nucleotide and predicted amino acid sequence of the A/Chile/1/83 NA exhibits a high homology with other N1 neuraminidases. Hyper-variable regions concerning A to G exchanges are discussed.

Amino Acid Sequence↗
PubMed1985

The effects of monoclonal antibodies against the hemagglutinin-neuraminidase and fusion protein on the release of Sendai virus from infected cells.

Vero cell cultures in Leighton tubes were infected with egg-grown Sendai virus at high multiplicity of infection. Four hours after infection, the cultures were labelled with 35S-methionine, after which various concentrations of fourteen and five mouse monoclonal antibodies directed against different antigenic determinants of the hemagglutinin-neuraminidase (HN) and fusion (F) protein, respectively, were added to the medium. Fourty-eight hours after infection radiolabelled virions released into the medium were collected and purified by discontinuous sucrose gradient centrifugations. The amount of virus-bound radioactivity obtained in the various extracellular materials allowed an estimation of the capacity of the different monoclonal antibodies to inhibit the release of Sendai virus. In addition, the release of virions from infected cells was studied ultrastructurally. Based on their serological reactivity the fourteen anti-HN monoclonal antibodies could be divided into four groups. The first group of clones could not inhibit any biological activity of the virus. These clones were binding proximally, near the base of the HN glycoprotein and could not inhibit the release of the virus. The second group blocked hemolysis, but did not block hemagglutination (HA) or neuraminidase (NA) activity. The third group of clones blocked all biological activities of the HN glycoprotein. The fourth group could only block NA activity. With the exception of one of five monoclonal antibodies belonging to the second group, antibodies of the second, third and fourth group were found to bind more distally on the HN glycoprotein. Except for two monoclonal antibodies of the second group they could all effectively inhibit release of the virus from infected cells. Ultrastructurally, these antibodies caused aggregation of virions in contact with the plasma membrane. The five monoclonal antibodies directed against the F protein reacted with four different antigenic sites. These antibodies could not prevent the release of Sendai virus.

Animals↗
PubMed1981

Comparative immunogenicity of live influenza viruses and their solubilized neuraminidases: results of mouse protection experiments.

Antigenicity and immunogenicity of three influenza virus strains A/PR/8/34 (H1N1). A/Hong Kong/1/68 (H3N2) and A/Port Chalmers/1/73 (H-3H2) were assayed comparatively with their corresponding neuraminidase isolated by proteolysis, and with the recombinant virus X-42 (Heq1 N2). It was concluded that intranasal immunization of mice with live virus induced heterologous immunity. Except in homologous neuraminidase-vaccinated mice, the subunit always was shown less effective and demonstrated a significantly lower antibody response than the corresponding whole virus.

Administration, Intranasal↗
PubMed1976

Interaction between the soluble and particulate neuraminidases of chick liver.

The sum of the neuraminidase activities found in the isolated soluble and particulate fractions of chick liver was considerably higher than that observed in the cytoplasmic extract from which these fractions were obtained. Addition of increasing amounts of particulate neuraminidase to a constant amount of the soluble preparation resulted in a progressive loss of enzyme activity.

Animals↗
PubMed1975

[Inhibition of bacterial neuraminidases by different anions (author's transl)].

It was shown that neuraminidase of Vibrio comma is inactivated by Ca..-binding anions like citrate, EDTA, oxalate, phosphate or tartrate. There is, however, no inhibition of the newly described enzymes of Erysipelothrix insidiosa and Streptococcus viridans. Pyruvate and, to a lesser extent, also citrate inactivate all the neuraminidases investigated independently of their activation by Ca..ions.

Ascorbic Acid↗
PubMed1983

Evidence for the contribution of the host species to the extent of antigenic variation of N1 influenza virus neuraminidase.

N1 influenza virus neuraminidases (NA) derived from avian, swine and human virus isolates, including the genetically related classic strains A/FPV/Rostock/34, A/Swine/1976/31, A/PR8/34 and A/FM1/47, were analysed serologically by neuraminidase inhibition (NI), inhibition of virus release (IVR) and competitive radio-immunoassays (competitive RIA). Comparing the three tests, competitive RIA appeared to be more reliable than NI and IVR for a quantitative assessment of antigenic relatedness. Together with evidence presented by others, these studies indicate that the host species contributes to the extent of antigenic variation of NAses. In contrast to NAses of human viruses where antigenic drift occurs readily, NAses of animal influenza viruses, from birds or mammalians, undergo far fewer antigen changes.

Animals↗
PubMed1990

Biochemical characteristics and subcellular localizations of rat liver neuraminidase isozymes: a paradox resolved.

A striking discrepancy in the abilities of two analytical approaches (fluorometric and electrophoretic) to detect the effect of a gene, Neu-2, on rat liver neuraminidase phenotypes led us to examine the biochemical and physical properties of the liver isozymes NEU-1 and NEU-2 that might be responsible for this difference. Cell fractionation via Percoll gradient centrifugation revealed NEU-1 activity almost exclusively in the lysosomal cell fraction, while NEU-2 was strictly cytosolic in distribution. The two isozymes were also found to differ in pH activity curves and optima (optima: 4.6-4.8 and 5.4-5.8 for NEU-1 and NEU-2, respectively) and in solubility characteristics (NEU-2 highly soluble; NEU-1 relatively insoluble but solubilized by freezing/thawing). Both isozymes were found to be freeze-thaw stable in crude, whole-cell extracts, but NEU-1 was destabilized in the enriched (partially purified) lysosomal subcellular fraction. Consideration of these properties relative to those described previously for unidentified cytosolic and membrane bound (lysosomal) rat liver neuraminidases (Tulsiani, D. R. P., and Carubelli, R., J. Biol. Chem. 245:1821, 1970) leads us to believe that NEU-2 also is destabilized by partial purification and that NEU-1 and NEU-2 have very different relative abundances within the cell. The biochemical and physical differences between NEU-1 and NEU-2 can account for the discrepant abilities of the fluorometric and electrophoretic approaches to detect the effects of Neu-2. Ways to increase the sensitivity of the fluorometric approach for quantitative assays of specific NEU-1 and NEU-2 activity are discussed.

Animals↗
PubMed1976

The use of a transesterification technique to distinguish between certain neuraminidase resistant epithelial mucins.

The effects of potassium hydroxide and soidum methoxide treatments upon the Alcian blue staining and neuraminidase lability of certain neuraminidase resistant epithelial mucins have been studied. The results were interpreted as indicating that while the mucins of rat colon and rabbit Brunner's gland contain only 4-0-acetyl sialic acid, human colonic epithelial mucins may contain some sialic acid with esters at the C1 carboxyl group.

Animals↗
PubMed2003

Neuraminidase inhibitors from Reynoutria elliptica.

In the course of screening neuraminidase inhibitors from herbal medicines, Reynoutria elliptica exhibited high inhibitory activity. Four active compounds were isolated from the ethyl acetate soluble fraction by consecutive purification using sillica gel, Sephadex LH-20 chromatography, and recrystallization. The chemical structures of these compounds were identified as 1,3,8-trihydroxy-6-methylanthraquinone (emodin) 1,8-dihydroxy-3-methoxy-6-methylanthraquinone (emodin 3-methyl ether; physcion), 1,3,8-trihydroxy-6-hydoxymethylanthraquinone (omega-hydroxyemodin), and 3,5,4'-trihydroxystilbene (trans-resvertrol) by spectral data including MS, 1H-, and 13C-NMR. The IC50 values of emodin, emodin 3-methyl ether, omega-hydroxyemodin, and trans-resvertrol were 2.81, 74.07, 10.49, and 8.77 microM, respectively. They did not inhibit other glycosidase such as glucosidase, mannosidase, and galactosidase, indicating that they were relatively specific inhibitors of neuraminidase.

Drugs, Chinese Herbal↗
PubMed2002

Early therapy with the neuraminidase inhibitor oseltamivir maximizes its efficacy in influenza treatment.

Influenza illness is an important cause of severe morbidity and mortality in the population. Oseltamivir, the first oral neuraminidase inhibitor, has proven efficacy. In children of 1 year and older (weight-dependent dosing: 30 mg, 45 mg, 60 mg or 75 mg BID for 5 days) and adults (75 mg BID for 5 days), oseltamivir reduces the duration and severity of acute influenza. Furthermore, it decreases the incidence of secondary complications such as otitis media, bronchitis, pneumonia and sinusitis. Oseltamivir has been shown to prevent influenza when given for long-term prophylaxis or for post-exposure prophylaxis. Because oseltamivir blocks the neuraminidase, an enzyme crucial to influenza virion liberation from the host cell, it is only effective during the replication phase. Clinical benefits are only seen, when oseltamivir is applied within 48 h after onset of symptoms, and clinical efficacy in acute influenza is highly dependent on the beginning of treatment. Treatment within 12 h after onset of symptoms reduces the duration of illness by an additional 74.6 h, and treatment within 24 hours an additional 53.9 h compared to the benefit seen with an intervention at 48 h. In conclusion, clinical efficacy of oseltamivir can be maximized by early start of treatment. Resistance of influenza virus against oseltamivir has rarely been observed and seems to be of no clinical relevance due to reduced transmissibility and pathogenicity of mutants. Oseltamivir is generally well tolerated. About 10% of the patients complain of transient upper gastrointestinal events, which resolved within 1-2 days, and which could be reduced when the medication was taken with a light snack.

Acetamides↗
PubMed2002

Exploitation of the Herpes simplex virus translocating protein VP22 to carry influenza virus proteins into cells for studies of apoptosis: direct confirmation that neuraminidase induces apoptosis and indications that other proteins may have a role.

Previously, we have shown that apoptosis induced by influenza virus was inhibited by an anti-neuraminidase compound [4-guanidino-2, 3-dehydro-N-acetylneuraminic acid (GG167; Relenza; Zanamivir)], which does not enter cells, and acts at the attachment/entry phase of virus replication. Furthermore, a virulent virus, clone 7a, induced greater levels of apoptosis than the attenuated A/Fiji and had greater neuraminidase (NA) activity. To confirm more directly that NA induces apoptosis, the NA of clone 7a and A/Fiji was expressed fused to the Herpes simplex virus tegument coat protein VP22, transfected into HeLa cells and the level of apoptosis determined. VP22 translocates between cells via the medium thus allowing expressed proteins to transfer to a larger number of cells than those originally transfected. Clone 7a NA fused to VP22 induced a significant level of apoptosis whereas A/Fiji NA/VP22 did not, confirming that NA activity is an important determinant of apoptosis acting during fusion protein translocation between cells. Furthermore, the induction of apoptosis was abrogated by antibody to transforming growth factor-beta, which is activated by NA. This approach also showed that VP22/NS1 proteins of both clone 7a and A/Fiji induced apoptosis when expressed alone but inhibited double stranded RNA-induced apoptosis suggesting that this protein may have a dual mode of action. Also, the M1 and M2 proteins of both viruses induced apoptosis but their NP proteins did not.

Apoptosis↗