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1.
Southeast Asian J Trop Med Public Health ; 2001 Mar; 32(1): 95-9
Article in English | IMSEAR | ID: sea-30787

ABSTRACT

The changes of drug susceptibilities of Vibrio cholerae O1 isolated during the past 7 years (1993-1999) in Lao PDR were investigated. The most noteworthy finding was the appearance of polymyxin B sensitive El Tor vibrios. Until 1996, the susceptibilities were almost as expected and cholera disappeared in 1997. When a cholera outbreak resurfaced in 1998, the susceptibilities of isolated V. cholerae O1 against tetracycline, sulfamethoxazol-trimethoprim, chloramphenicol and polymyxin B were quite different from those of previously isolated organisms. Minimum inhibitory concentrations (MICs) of tetracycline and chloramphenicol against the isolates in 1998 were about 16 times higher than those against the previous isolates, and the MICs of sulfamethoxazol-trimethoprim were about 256 times higher than those against the previous isolates, (trimethoprim 32 microg/ml: sulfamethoxazol 608 microg/ml). Eleven percent of the isolates (11/99) were as sensitive to polymyxin B as the classic cholera vibrios (MIC < 2 microg/ml). In 1999, the susceptibility pattern was almost the same as that in 1998 except for polymyxin B to which 58% of the isolates (21/36) became sensitive.


Subject(s)
Anti-Bacterial Agents/pharmacology , Cholera/drug therapy , Disease Outbreaks , Drug Resistance, Microbial , Humans , Laos/epidemiology , Microbial Sensitivity Tests , Vibrio cholerae/drug effects
2.
Southeast Asian J Trop Med Public Health ; 2000 Jun; 31(2): 360-5
Article in English | IMSEAR | ID: sea-35217

ABSTRACT

Pilus of Vibrio parahaemolyticus O3:K6 strain LVP9 belonging to the newly identified clone was purified and characterized. The molecular mass of the pilin was estimated to be about 18 kDa by SDS-PAGE, and the isoelectric point of the pilin was 5.0 +/- 0.2. The LVP9 pili were antigenically different from the other V. parahaemolyticus Na2 pili and Ha7 pili as previously reported, nevertheless all three had indistinguishable morphology and shared a high degree of homology in their N-terminal amino acid sequences. Strain LVP9 and its purified pili did not agglutinate human and rabbit erythrocytes. The LVP9 organisms and the purified pili were adhesive to the rabbit intestine. The adhesion was inhibited by pretreatment of the rabbit intestine with the purified pili or by pretreatment of the organisms with the Fab fractions of anti-pilus antibody. These results indicate that the LVP9 pilus is an adherent factor to the rabbit intestine.


Subject(s)
Amino Acid Sequence , Bacterial Adhesion , Fimbriae Proteins , Fimbriae, Bacterial/chemistry , Hemagglutination , Isoelectric Point , Membrane Proteins/chemistry , Microscopy, Immunoelectron , Molecular Sequence Data , Molecular Weight , Serotyping , Vibrio parahaemolyticus/classification
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