{"title":"An evaluation of allozyme amino acid substitutions for the study of molecular relationships in Providencia strains","authors":"P Goullet , B Picard , R Krishnamoorthy","doi":"10.1016/0769-2609(88)90074-9","DOIUrl":"10.1016/0769-2609(88)90074-9","url":null,"abstract":"<div><p>Through analysis of molecular relationships in terms of amino acid substitutions, intra- and interspecies differentiations in <em>Providencia alcalifaciens</em>, <em>P. stuartii</em> and <em>P. rustigianii</em> were evaluated among the electrophoretic variants of three enzymes, L-malate dehydrogenase, acid phosphatase and esterase-βa, chosen for their distinct pattern of polymorphism. For each enzyme, molecular relatedness among variants defined by two-dimensional electrophoretic profiles was examined through protein titration curves. <em>P. stuartii</em> strains appeared identical to each other and <em>P. rustigianii</em> strains were closely related, whereas the division of <em>P. alcalifaciens</em> strains into previously described zymotypes A<sub>1</sub> and A<sub>2</sub> was refined in molecular terms. A gradient of molecular interrelatedness between the species was observed for the three enzyme loci: with L-malate dehydrogenase, the three species appeared very closely related; with acid phosphatase, <em>P. stuartii</em> and <em>P. alcalifaciens</em> were more closely related to each other than to <em>P. rustigianii</em>; with esterase-βa, <em>P. alcalifaciens</em> and <em>P. stuartii</em> appeared partially related, whereas no such relatedness was observed between these two species and <em>P. rustigianii</em>.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Pages 689-702"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90074-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14379608","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The envelope structure of Branhamella catarrhalis as studied by transmission electron microscopy","authors":"R Hellio , M Guibourdenche , E Collatz , J.Y Riou","doi":"10.1016/0769-2609(88)90151-2","DOIUrl":"10.1016/0769-2609(88)90151-2","url":null,"abstract":"<div><p>The envelope structure of <em>Branhamella catarrhalis</em> was studied by electron microscopy and compared with that of other bacteria of the family <em>Neisseriaceae</em>, such as <em>Moraxella lacunata</em> subsp. <em>liquefaciens</em> and <em>Neisseria gonorrhoeae</em>.</p><p>Negative staining of <em>B. catarrhalis</em> showed a mamilliform surface similar to that of <em>Moraxella</em>. On thin sections, the cell wall appeared to be made up of a wavy outer membrane tightly linked to a straight peptidoglycan layer. Spicule-like structures protruded from the cell surface. Ruthenium red staining revealed that they contained polysaccharides. While the outer polysaccharide layer of <em>N. gonorrhoeae</em> was unstable after repeated subcultures <em>in vitro</em>, this layer remained stable in <em>B. catarrhalis</em> and in <em>Moraxella lacunata</em> subsp. <em>liquefaciens</em>.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 5","pages":"Pages 515-525"},"PeriodicalIF":0.0,"publicationDate":"1988-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90151-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13618041","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M Archambaud , P Courcoux , V Ouin , G Chabanon , A Labigne-Roussel
{"title":"Phenotypic and genotypic assays for the detection and identification of adhesins from pyelonephritic Escherichia coli","authors":"M Archambaud , P Courcoux , V Ouin , G Chabanon , A Labigne-Roussel","doi":"10.1016/0769-2609(88)90155-X","DOIUrl":"10.1016/0769-2609(88)90155-X","url":null,"abstract":"<div><p>Four different gene clusters have been characterized so far which encode adhesins involved in the specific binding of pathogenic <em>Escherichia coli</em> to epithelial cells of the urinary tractus: the <em>pap, sfa, afa</em> and <em>bma</em> operons. The ability to adhere to uroepithelial cells and to interact with one or several of the specific receptors identified for each of the 4 adhesins, has been studied for 102 <em>E. coli</em> strains isolated from patients with pyelonephritis. These receptor-binding assays are referred to as phenotypic assays. Isolates which adhered to uroepithelial cells 68.6% produced at least 1 of the previously described adhesins. In addition, we used DNA probes to detect homologous sequences of the <em>pap, sfa</em> and <em>afa</em> operons. Genotypic assays revealed that 87.2 % of pyelonephretic <em>E. coli</em> contain DNA sequences related to at least 1 of the 4 operons; 78.4 %, 22.5 % and 11.8 % of the strains harboured sequences related to <em>pap, sfa</em> and <em>afa</em> operons, respectively. The <em>afa</em>- and <em>sfa</em>- adhesion determinants were commonly found associated with the presence of the <em>pap</em> operon (8.8 % and 18.6 %, respectively). Detection of adhesins using the genotypic approach appears to be reliable (all adhesins detected using the phenotypic approach were also detected with probes). Detection by colony hybridization was significantly higher than by phenotypic assay. Discrepancies may have been due to absence of expression of the detected operons and may have resulted from improper <em>in vitro</em> growth conditions, phase variation, and/or heterogeneity of the genes encoding the adhesins within a family of related sequences.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 5","pages":"Pages 557-573"},"PeriodicalIF":0.0,"publicationDate":"1988-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90155-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13993490","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Specificity of Mycobacterium tuberculosis phenolic glycolipid (PGL-Tb1) antiserum","authors":"F Papa , A Laszlo , H.L David","doi":"10.1016/0769-2609(88)90153-6","DOIUrl":"10.1016/0769-2609(88)90153-6","url":null,"abstract":"<div><p>The specificity of <em>Mycobacterium tuberculosis</em> anti-PGL-Tb1 antiserum prepared in rabbits was evaluated by an enzyme-linked immunosorbent assay. It was found that the antiserum immunoreacted with its homologous antigen but not with purified phenolic glycolipids from <em>M. bovis</em> BCG (mycoside B), <em>M. kansasii</em> (mycoside A), <em>M. leprae</em> (PGL-I) or <em>M. marinum</em> (mycoside G).</p><p>The analysis of chloroform/methanol extracts from 15 strains of <em>M. tuberculosis</em> showed that all formed the antigen except the type strain (strain H37Rv). Chloroform/methanol extracts of <em>M. bovis</em> BCG, <em>M. xenopi, M. flavescens</em> and <em>M. fallax</em> cross-reacted with the immune serum. However, chloroform/methanol extracts of representative strains of 18 other mycobacterial species did not reach, therefore indicating that these did not contain the antigen.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 5","pages":"Pages 535-545"},"PeriodicalIF":0.0,"publicationDate":"1988-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90153-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13618043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Prix du gremi","authors":"","doi":"10.1016/0769-2609(88)90176-7","DOIUrl":"https://doi.org/10.1016/0769-2609(88)90176-7","url":null,"abstract":"","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 5","pages":"Page A3"},"PeriodicalIF":0.0,"publicationDate":"1988-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90176-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137200759","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}