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1.
Clin Diagn Lab Immunol ; 4(5): 536-9, 1997 Sep.
Article in English | MEDLINE | ID: mdl-9302201

ABSTRACT

Serum and stool samples were collected from 128 individuals: 96 diarrhea patients and 32 apparently healthy controls. Stool specimens were cultured for enteric bacterial pathogens, while sera were screened by enzyme-linked immunosorbent assay for Campylobacter jejuni-reactive antibodies. Of 28 diarrhea patients who demonstrated C. jejuni-reactive antibodies (titers, > 100), 14 were culture positive for this organism. The 32 healthy controls showed significantly lower antibody titers (P < 0.05) with the exception of 10 subjects who were culture positive for C. jejuni and had reactive immunoglobulin M (IgM) (6 subjects) and IgG (7 subjects). IgA was not detected in those 10 individuals (asymptomatic). Avidity was expressed as the thiocyanate ion concentration required to inhibit 50% of the bound antibodies. The avidity was higher in symptomatic patients than asymptomatic healthy controls. IgG was less avid (0.92 M) compared to IgM (0.1 M) and IgA (1.1 M), with no correlation between antibody titer and avidity. However, the thiocyanate ion concentration required for the complete inhibition of IgG (5 M)-bound antibodies was higher than that of IgA (2 M) and IgM (3 M). This study also shows that C. jejuni antibodies were variably cross-reactive with Escherichia coli, Shigella flexneri, Shigella sonnei, and Neisseria meningitidis in addition to Campylobacter coli and Campylobacter rectus.


Subject(s)
Antigens, Bacterial/analysis , Campylobacter Infections/immunology , Campylobacter jejuni/immunology , Diarrhea/immunology , Antigen-Antibody Reactions , Developing Countries , Diarrhea/microbiology , Enzyme-Linked Immunosorbent Assay , Humans , Immunoglobulin A/analysis , Immunoglobulin G/analysis , Immunoglobulin M/analysis
2.
J Bacteriol ; 176(24): 7476-83, 1994 Dec.
Article in English | MEDLINE | ID: mdl-8002570

ABSTRACT

Many of the gene products that participate in nitrogen metabolism are sensitive to nitrogen catabolite repression (NCR), i.e., their expression is decreased to low levels when readily used nitrogen sources such as asparagine are provided. Previous work has shown this NCR sensitivity requires the cis-acting UASNTR element and trans-acting GLN3. Here, we extend the analysis to include the response of their expression to deletion of the URE2 locus. The expression of these nitrogen catabolic genes becomes, to various degrees, NCR insensitive in the ure2 deletion. This response is shown to be mediated through the GATAA-containing UASNTR element and supports the current idea that the NCR regulatory circuit involves the following steps: environmental signal-->URE2-->GLN3-->UASNTR operation-->NCR-sensitive gene expression. The various responses of the nitrogen catabolic genes' expression to deletion of the URE2 locus also indicate that not all NCR is mediated through URE2.


Subject(s)
Fungal Proteins/genetics , Gene Expression Regulation, Fungal , Nitrogen/metabolism , Prions , Regulatory Sequences, Nucleic Acid/genetics , Saccharomyces cerevisiae Proteins , Saccharomyces cerevisiae/genetics , Allantoin/metabolism , Amino Acids/metabolism , Base Sequence , Biological Transport/genetics , Gene Deletion , Genes, Fungal/genetics , Genes, Reporter , Glutathione Peroxidase , Molecular Sequence Data , Proline/metabolism , Promoter Regions, Genetic/genetics , Transcription, Genetic , gamma-Aminobutyric Acid/metabolism
3.
J Bacteriol ; 175(1): 64-73, 1993 Jan.
Article in English | MEDLINE | ID: mdl-8416910

ABSTRACT

We demonstrate that expression of the UGA1, CAN1, GAP1, PUT1, PUT2, PUT4, and DAL4 genes is sensitive to nitrogen catabolite repression. The expression of all these genes, with the exception of UGA1 and PUT2, also required a functional GLN3 protein. In addition, GLN3 protein was required for expression of the DAL1, DAL2, DAL7, GDH1, and GDH2 genes. The UGA1, CAN1, GAP1, and DAL4 genes markedly increased their expression when the DAL80 locus, encoding a negative regulatory element, was disrupted. Expression of the GDH1, PUT1, PUT2, and PUT4 genes also responded to DAL80 disruption, but much more modestly. Expression of GLN1 and GDH2 exhibited parallel responses to the provision of asparagine and glutamine as nitrogen sources but did not follow the regulatory responses noted above for the nitrogen catabolic genes such as DAL5. Steady-state mRNA levels of both genes did not significantly decrease when glutamine was provided as nitrogen source but were lowered by the provision of asparagine. They also did not respond to disruption of DAL80.


Subject(s)
DNA-Binding Proteins/genetics , Fungal Proteins/genetics , Gene Expression Regulation, Fungal , Genes, Fungal/genetics , Repressor Proteins , Saccharomyces cerevisiae Proteins , Saccharomyces cerevisiae/genetics , Transcription Factors , Allantoin/pharmacology , Asparagine/pharmacology , Base Sequence , GATA Transcription Factors , Gene Deletion , Glutamine/pharmacology , Models, Genetic , Molecular Sequence Data , Nitrogen/metabolism , Proline/pharmacology , RNA, Messenger/analysis , Regulatory Sequences, Nucleic Acid/genetics , Saccharomyces cerevisiae/metabolism , gamma-Aminobutyric Acid/pharmacology
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