{"title":"Molecular mechanisms of methicillin resistance in Staphylococcus aureus.","authors":"M A Domínguez, J Liñares, R Martín","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Methicillin-resistant Staphylococcus aureus (MRSA) strains are among the most common nosocomial pathogens. The most significant mechanism of resistance to methicillin in this-species is the acquisition of a genetic determinant (mecA gene). However, resistance seems to have a more complex molecular basis, since additional chromosomal material is involved in such resistance. Besides, overproduction of penicillinase and/or alterations in the PBPs can contribute to the formation of resistance phenotypes. Genetic and environmental factors leading to MRSA are reviewed.</p>","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"301-8"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20284690","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}
L Sánchez, S Leranoz, M Puig, J G Lorén, H Nikaido, M Viñas
{"title":"Molecular basis of antimicrobial resistance in non-typable Haemophilus influenzae.","authors":"L Sánchez, S Leranoz, M Puig, J G Lorén, H Nikaido, M Viñas","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Strains of the facultative anaerobe Haemophilus influenzae, both type b and non typable strains, are frequently multiresistant. The measurement of the antibiotic permeability of Haemophilus influenzae outer membrane (OM) shows that antibiotics can cross through the OM easily. Thus, enzymatic activity or efflux pumps could be responsible for multiresistance. An efflux system closely related to AcrAB of Escherichia coli is present in Haemophilus influenzae. However, their role in multiresistance seems irrelevant. Classical mechanisms such as plasmid exchange seems to be playing a major role in the multidrug resistance in Haemophilus influenzae.</p>","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"309-14"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20284691","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 role of outer membrane in Serratia marcescens intrinsic resistance to antibiotics.","authors":"L Sánchez, N Ruiz, S Leranoz, M Viñas, M Puig","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Three different porins from Serratia marcescens were described. They were named Omp1, Omp2 and Omp3 and their molecular weights were 42, 40 and 39 kDa respectively. Omp2 and Omp3 showed osmoregulation and thermoregulation in a similar way to OmpC and OmpF of Escherichia coli. Permeability coefficients of the outer membrane of this species were calculated following the Zimmermann and Rosselet method. P values were similar to those obtained in Escherichia coli, which suggests that the chromosomal beta-lactamase would play a major role in the resistance of Serratia marcescens to beta-lactam antibiotics. Both MIC values and permeabilities were modified by salycilates and acetylsalycilate. Synergism between the outer membrane and the beta-lactamase was also evaluated. When bacteria grew in the presence of a beta-lactam in the medium, the beta-lactamase accounted for most of the resistance.</p>","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"315-20"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20284692","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":"Resistance to antivirals in human cytomegalovirus: mechanisms and clinical significance.","authors":"J L Pérez","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Long term therapies needed for managing human cytomegalovirus (HCMV) infections in immunosupressed patients provided the background for the emergence of the resistance to antivirals active against HCMV. In addition, laboratory selected mutants have also been readily achieved. Both clinical and laboratory resistant strains share the same determinants of resistance. Ganciclovir resistance may be due to a few mutations in the HCMV UL97 gene and/or viral DNA pol gene, the former being responsible for about 70% of clinical resistant isolates. Among them, V464, V594, S595 and F595 are the most frequent mutations. Because of their less extensive clinical use, much less is known about resistance to foscarnet and cidofovir (formerly, HPMPC) but in both cases, it has been associated to mutations in the DNA pol. Ganciclovir resistant strains showing DNA pol mutations are cross-resistant to cidofovir and their corresponding IC50 are normally higher than those from strains harboring only mutations at the UL97 gene. To date, foscarnet resistance seems to be independent of both ganciclovir and cidofovir resistance.</p>","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"343-52"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20284696","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":"Moderate resistance to penicillin in Neisseria meningitidis.","authors":"J A Sáez Nieto, J A Vázquez","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Meningococcal moderate resistance to penicillin (MICs 0.12 to 1 mg/l) was rarely reported before the 1980's in Spain. The frequency of isolation of resistant strains increased from 0.4% in 1985 to 42.6% in 1990. In the last few years, these strains have been reported in several countries, which suggests a change in the meningococcal response to penicillin. The resistance is due, at least in part, to a decreased affinity of penicillin binding protein 2 (PBP2) for penicillin. This decreased affinity has also been found in commensal Neisseriae. Population genetic studies demonstrate that recombinational events, replacing parts of the PBP2 gene by the corresponding regions of commensal species, followed by a rapid spread of the clones could be the origin of such resistant strains.</p>","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"337-42"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20284695","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":"[Trajectory and current situation of biomedical research in Argentina].","authors":"S M González Cappa","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"267-70"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20353668","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 Hernández, F J Carrera, C L Ronchera, M A Ferrús, J Hernández
{"title":"[Microbiology and the Internet].","authors":"M Hernández, F J Carrera, C L Ronchera, M A Ferrús, J Hernández","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"363-70"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20353669","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":"Purification of OmpU from Vibrio cholerae classical strain 569B: evidence for the formation of large cation-selective ion-permeable channels by OmpU.","authors":"R Benz, E Maier, T Chakraborty","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The outer membrane of the classical Vibrio cholerae strain 569B was isolated by sucrose density centrifugation. The simple treatment of the isolated outer membrane or the cell envelopes with different detergents allowed the purification of two outer membrane proteins, the 38 kDa OmpU and the 25 kDa OmpV. Furthermore, a 35 kDa outer membrane protein (probably the 35 kDa OmpA-like protein) was purified by two-fold treatment of the cell envelope with 2% SDS solution. A subsequent wash of the SDS-pellet with 2% Genapol buffer yielded in the 38 kDa OmpU protein, which formed SDS-resistant oligomers (66 kDa). The Genapol pellet contained OmpV. Reconstitution experiments with lipid bilayer membranes demonstrated that OmpU was a channel-forming component, whereas OmpV had a small channel-forming ability if any. The OmpU channels appeared to be large and water-filled and had a single-channel conductance of about 2 nS in 1 M KCl for the monomer in a trimer, which means that they have a larger cross-section than enterobacterial porins. The channels showed rapid switching between open and closed configuration. They were slightly cation-selective, which suggests that they contain an excess of negatively charged amino groups.</p>","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"321-30"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20284693","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":"Sergei I. Kuznetsov (1900-1987). The founder of Russian aquatic microbiology.","authors":"N N Lyalikova, V M Gorlenko","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77263,"journal":{"name":"Microbiologia (Madrid, Spain)","volume":"13 3","pages":"353-6"},"PeriodicalIF":0.0,"publicationDate":"1997-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20284697","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}