Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0149514 (bronchitis)
 6,902 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polymerase chain reaction (PCR) and restriction fragment length polymorphism (RFLP) analysis were used to differentiate between serotypes of several infectious bronchitis virus (IBV) strains. A sequence of 1720 base pairs (bp) that contains the S1 glycoprotein gene of IBV was amplified by PCR, purified, and digested with restriction enzymes. Eleven reference IBV strains were grouped according to the RFLP patterns. The IBV Holte, Arkansas DPI, SE 17, Md 27, and Iowa 97 strains could be differentiated from the other IBV strains using the restriction enzyme HaeIII. The Beaudette, Massachusetts 41, Connecticut, and Florida 88 strains had the same HaeIII RFLP pattern but could be differentiated using XcmI and BstYI restriction enzymes. The Gray and JMK strains could not be differentiated by their RFLP patterns following digestion with 23 different restriction enzymes. Twenty-six samples (field isolates and reference strains) of IBV, previously serotypes by the virus-neutralization (VN) test in embryonating eggs, were analyzed in a blind fashion. The results using the PCR and RFLP analysis agreed with the serotype for traditional and variant IBV viruses as determined by the VN test.
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PMID:Differentiation of infectious bronchitis virus serotypes using polymerase chain reaction and restriction fragment length polymorphism analysis. 809 82

Coronaviruses (CV) infect a variety of livestock, poultry and companion animals. They belong to at least five antigenic groups. CV cause localized infections of the respiratory and/or intestinal tracts, with the exception of feline infectious peritonitis virus (FIPV) and hemagglutinating encephalomyelitis (HEV) which cause systemic infections. The enteropathogenic CV infect the villous enterocytes resulting in villous atrophy leading to malabsorptive diarrhea. Several CV (bovine CV-BCV, porcine respiratory CV-PRCV, infectious bronchitis virus-IBV) cause respiratory disease. Current evidence indicates that protection against enteric and respiratory CV infections is mediated by passive or active immunity at the primary site of CV replication. Maternal vaccination approaches to induce passive immunity include the use of inactivated and modified live viral vaccines. Modified live viruses and a Ts mutant CV (FIPV) are also used as oral or intranasal vaccines to induce active mucosal immunity. The success of these vaccines in the field is often compromised by a number of potential problems. Coronaviruses are spherical, enveloped viruses, ranging from 80-160 nm in diameter and containing a positive-stranded RNA genome. They possess prominent surface spikes and some species display a fringe of smaller surface projections believed to be the hemagglutinin (HE). Coronaviruses possess 3 to 4 structural proteins: the spike (S) glycoprotein (150-200 kDa), the integral membrane glycoprotein (M; 20-30 kDa) and the nucleocapsid phosphoprotein (N; 43-50 kDa). A subset of CV (BCV, HEV, turkey CV) possess a third glycoprotein on the virion surface, the HE (60-65 kDa). These proteins can be quantitated using pooled monoclonal antibodies (mAb) to distinct epitopes of each protein in ELISA. Most research has focused on the S protein as a candidate antigen for CV vaccines since it induces virus neutralizing (VN) antibodies. However the HE protein stimulates the production of VN and HE inhibiting antibodies and the M protein induces antibodies that neutralize virus in the presence of complement. Attempts to correlate in vitro VN antibody activity with in vivo protection have shown that the passive transfer of VN mAb to the S or HE protein conferred passive protection against CV challenge in some studies, but not others. Additional research has implicated a possible role for other CV proteins in immunity. Studies of mAb to the M protein of transmissible gastroenteritis (TGEV) have provided evidence for a direct role of the M protein in the induction of alpha IFN by porcine blood leukocytes. The potential significance of this phenomenon to immunity to TGEV is unclear.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Coronavirus immunogens. 811 87

Seaprose is a semialkaline proteinase endowed with proteolytic effect and antiinflammatory activity tested in different clinical trials. There is clinical evidence that seaprose reduces sputum viscoelastic properties in chronic hypersecretory bronchitis. The present study evaluated (in a double-blind design vs. placebo) the activity of seaprose on bronchial inflammation, mucus glycoprotein secretion and bronchial humoral defence mechanism in chronic bronchitic patients clinically stable (10 per group). Markers of bronchial inflammation (albumin, albumin/total protein ratio) and bronchial infection (DNA), of mucus glycoproteins (fucose and N-acetylneuraminic acid) and of humoral defence mechanism (secretory-IgA) were tested in sputum. We found that ten-day treatment with seaprose (90 mg/day) reduced sputum albumin during the observation period, the difference being statistically significant at the 18th day. The sputum albumin/total protein ratio also decreased by 50% at the end of the study. In the same group, sputum DNA, secretory-IgA, fucose and N-acetylneuraminic acid remained unchanged after treatment. The placebo group did not show any significant changes in the sputum marker substances. This study provides experimental evidence for the antiinflammatory activity of seaprose on bronchial mucosa in chronic bronchitic patients studied in a stable phase of their disease. Furthermore the drug does not seem to affect mucus glycoprotein secretion or secretory-IgA production.
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PMID:Effects of seaprose on sputum biochemical components in chronic bronchitic patients: a double-blind study vs placebo. 820 Jul 22

The antigenicity of the S1, M and N proteins of avian infectious bronchitis virus was compared following immunization of chickens with live and inactivated virus. The N protein was immunodominant antigen inducing cross-reactive antibodies in high titres whereas the S1 glycoprotein induced serotype-specific and cross-reactive antibodies. The M glycoprotein elicited antibodies in low titres and of limited cross-reactivity. Immunization of chickens with the purified N and M proteins did not induce protection against virulent challenge whereas immunization with the S1 glycoprotein prevented replication of nephropathogenic IBV in kidneys but not in tracheas of immunized chickens.
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PMID:Structural proteins of avian infectious bronchitis virus: role in immunity and protection. 820 67

In infectious bronchitis (IB) virus infection of the chicken the upper and lower respiratory tracts were damaged, but infectious laryngotracheitis (ILT) virus caused lesions only in the upper respiratory tract. Secondary infection with Escherichia coli was apparent in the trachea of birds inoculated with either virus but was more striking in those given IB virus. Serum alpha 1-acid glycoprotein, an acute-phase protein, occurred in higher concentrations in chickens inoculated with IB virus than in those given ILT virus.
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PMID:Comparison of the effects of infectious bronchitis and infectious laryngotracheitis on the chicken respiratory tract. 872 76

Synthetic peptides were prepared as multiple antigenic peptide (MAP) constructs to the S1 glycoprotein of infectious bronchitis virus (IBV). The MAP system has been used in the production of anti-peptide and anti-protein antibodies. It has an advantage over linking peptides to a highly immunogenic carrier molecule because antibodies are not produced to the MAP core matrix of lysine residues. Two 25-residue peptides were synthesized to the Arkansas serotype and two were synthesized to the Massachusetts serotype of IBV. The peptide sequences correspond to amino acid residues 64 to 88 and to residues 117 to 141 for each of the IBV serotypes. A MAP construct for each peptide was prepared by linking 4 copies of a peptide to the immunogenetically inert core matrix of lysine residues. The MAP constructs were used to immunize specific pathogen free chickens. Anti-peptide ELISA titers and the dot immunobinding assay against the homologous peptide were positive for all of the sera tested whereas the anti-whole virus ELISA titers and virus neutralization titers were negative for all of the sera tested. Hyperimmune sera against whole virus did not cross react with synthetic peptides made to the heterologous virus suggesting a possible role for the MAP constructs in a serotype specific dot blot or ELISA test for IBV.
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PMID:Production and immunogenicity of multiple antigenic peptide (MAP) constructs derived from the S1 glycoprotein of infectious bronchitis virus (IBV). 883 Apr 82

The M glycoprotein from the avian coronavirus, infectious bronchitis virus (IBV), contains information for localization to the cis-Golgi network in its first transmembrane domain. We hypothesize that localization to the Golgi complex may depend in part on specific interactions between protein transmembrane domains and membrane lipids. Because the site of sphingolipid synthesis overlaps the localization of IBV M, we asked whether perturbation of sphingolipids affected localization of IBV M. Short-term treatment with two inhibitors of sphingolipid synthesis had no effect on localization of IBV M or other Golgi markers. Thus, ongoing synthesis of these lipids was not required for proper localization. Surprisingly, a third inhibitor, d,l-threo-1-phenyl-2-decanoylamino-3-morpholino- 1-propanol (PDMP), shifted the steady-state distribution of IBV M from the Golgi complex to the ER. This effect was rapid and reversible and was also observed for ERGIC-53 but not for Golgi stack proteins. At the concentration of PDMP used, conversion of ceramide into both glucosylceramide and sphingomyelin was inhibited. Pretreatment with upstream inhibitors partially reversed the effects of PDMP, suggesting that ceramide accumulation mediates the PDMP-induced alterations. Indeed, an increase in cellular ceramide was measured in PDMP-treated cells. We propose that IBV M is at least in part localized by retrieval mechanisms. Further, ceramide accumulation reveals this cycle by upsetting the balance of anterograde and retrograde traffic and/ or disrupting retention by altering bilayer dynamics.
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PMID:Ceramide accumulation uncovers a cycling pathway for the cis-Golgi network marker, infectious bronchitis virus M protein. 939 47

Golgi resident proteins maintain their localization despite a continual protein and lipid flux through the organelle. To study Golgi retention mechanisms, we have focused upon the chimeric protein Gm1. This protein contains the Golgi transmembrane domain targeting signal from the infectious bronchitis virus M protein and the lumenal and cytoplasmic domain of the vesicular stomatitis virus glycoprotein (VSV G). The Gm1 protein is targeted to the Golgi where it forms an unusually stable detergent-resistant oligomer. The formation of oligomeric structures may aid retention of Golgi resident proteins. Thus, determining the stabilization mechanism may shed light on Golgi protein retention. Previous work determined that the transmembrane domain is required for the targeting and oligomerization of Gm1, but it is the cytoplasmic tail that stabilizes the complexes [Weisz, O. A., Swift, A. M., and Machamer, C. E. (1993) J. Cell Biol. 122, 1185-1196]. However, further study of the oligomer has been difficult due to its insolubility. Here we report that fragmenting the Gm1 protein into several pieces facilitates solubilization by sodium dodecyl sulfate (SDS). By analyzing the fragments produced after cleavage, we determined that the stability of the oligomer is not caused by covalent linkage of Gm1 to itself or other proteins. The fragment corresponding to the transmembrane domain and tail of Gm1 had an enhanced mobility in SDS gels relative to the same fragment of the parent VSV G protein. The enhanced migration of the tail fragment does not reflect sequence differences or post-translational modification, but correlates with Golgi localization and oligomerization. We suggest that the enhanced mobility of the Gm1 tail fragment reflects an altered conformation which serves to stabilize the detergent-resistant oligomers.
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PMID:Fragmentation of a Golgi-localized chimeric protein allows detergent solubilization and reveals an alternate conformation of the cytoplasmic domain. 942 38

A recombinant baculovirus containing the S1 glycoprotein gene of the virulent nephropathogenic KM91 strain of infectious bronchitis virus (IBV) was constructed in order to investigate protective immunity in vaccinated chickens. Results from the protection test were evaluated by re-isolation of virus from the kidneys and tracheas of vaccinated chickens after challenge with strain KM91. After three immunizations, the recombinant S1 (rS1) glycoprotein induced 50% protection of the kidney, whilst inactivated KM91 induced 88% and 50% protection of the kidney and trachea, respectively. In chickens primed with the attenuated H120 vaccine strain, which is heterologous to KM91, the rS1 glycoprotein induced 83% protection of the kidney after two immunizations. Haemagglutination-inhibition titres were also increased in chickens immunized with the rS1 glycoprotein after three immunizations, and significantly higher titres were detected after challenge. These data indicate that the expressed rS1 glycoprotein alone can induce a protective immune response as well as an antibody response.
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PMID:Induction of protective immunity in chickens vaccinated with infectious bronchitis virus S1 glycoprotein expressed by a recombinant baculovirus. 956 66

The glycoprotein (15-18 kDa) antigen of Mycobacterium tuberculosis H37Rv was affinity isolated on the immunosorbent with monoclonal antibodies S4C1G4 (specific to M. tuberculosis H37Rv; Avdiyenko V. G., Kondrashov S.Yu, Lyashenko S.M.@Probl. Tuberk. 1996, v. 1, p. 6-8 (in Russian). This antigen and PPD (Batch RT 45, Stattens Seruminstitute, Denmark) that was a standard antigen were used for enzyme-linked immunosorbent assay (ELISA), by detecting serum IgG antibodies in patients with pulmonary tuberculosis, and control groups of patients with lung diseases other than tuberculosis (bronchitis and/or asthma, pneumonia) as well as healthy volunteers. The diagnostic parameters of specificity and sensitivity for titers and the same parameters for optic density (OD) (in serum dilution with maximum differences for groups of patients and donors) were compared. The new monoantigen method provided 86.11% specificity and 87.87% sensitivity, which were higher those obtained for optic density (63.89 and 80%, respectively). With PPD, the specificity and sensitivity were 58.04 and 78.78 (for the new titer method) versus 50 and 78.78% (OD data). The method error for titer determination was 10% and for standard OD determination was 27%. The new approach offers additional possibilities of enhancing the quality of ELISA for diagnosis of tuberculosis.
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PMID:[Comparative analysis of two mycobacterium tuberculosis antigens and two methodological approaches to determining serum antimycobacterial antibodies]. 961 81


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