No abstract available.
Plasmids* ; Shigella* ; Virulence Factors* ; Virulence*

No Abstract Available.
Vibrio parahaemolyticus* ; Vibrio* ; Virulence Factors* ; Virulence*

No Abstract Available.
Vibrio parahaemolyticus* ; Vibrio* ; Virulence Factors* ; Virulence*

No abstract available.
Escherichia coli* ; Escherichia* ; HeLa Cells* ; Humans ; Virulence Factors* ; Virulence*

Monospecific B.pertussis antisera prepared at IVAC, Nha Trang, Da Lat have been used in the identifying testing for the presence of agglutinogens 1, 2 and 3 in B.pertussis strains GL353, 360E, H36, 248, 305, 18323 and in vaccine final bulks L617, L617-636, L624-628, L627-634, L634-636, L613-614. Similar results were obtained with monospecific B.pertussis antisera issued by the United Kingdom.
Virulence Factors, Bordetella ; Bordetella pertussis ; Immune Sera

Fungi ; Humans ; Rhinitis, Allergic/therapy* ; Virulence Factors

PURPOSE: There is a need to broaden protective coverage of M protein–based vaccines against group A streptococci (GAS) because coverage of the current 30-valent M protein vaccine does not extend to all emm types. An additional GAS antigen and virulence factor that could potentially extend vaccine coverage is M-related protein (Mrp). Previous work indicated that there are three structurally related families of Mrp (MrpI, MrpII, and MrpIII) and peptides of all three elicited bactericidal antibodies against multiple emm types. The purpose of this study was to determine if a recombinant form containing Mrp from the three families would evoke bactericidal antiserum and to determine if this antiserum could enhance the effectiveness of antisera to the 30-valent M protein vaccine. MATERIALS AND METHODS: A trivalent recombinant Mrp (trMrp) protein containing N-terminal fragments from the three families (trMrp) was constructed, purified and used to immunize rabbits. Anti-trMrp sera contained high titers of antibodies against the trMrp immunogen and recombinant forms representing MrpI, MrpII, and MrpIII. RESULTS: The antisera opsonized emm types of GAS representing each Mrp family and also opsonized emm types not covered by the 30-valent M protein–based vaccine. Importantly, a combination of trMrp and 30-valent M protein antiserum resulted in higher levels of opsonization of GAS than either antiserum alone. CONCLUSION: These findings suggest that trMrp may be an effective addition to future constructs of GAS vaccines.
Antibodies ; Humans ; Immune Sera ; Peptides ; Rabbits ; Staphylococcal Protein A* ; Streptococcal Vaccines* ; Streptococcus pyogenes ; Vaccines ; Virulence ; Virulence Factors

A total of 100 Vibrio spp. strains were examined for production of various extracellular enzyme and for plasmid content plasmid were subjected to digestion with restriction enzymes. Most of them produced extracellular enzyme more than one, especially V. parahaemolyticus and V. cholerae non-01 strains were showed production of various extracellular enzymes. About the 55% Vibrio spp. have the plasmid more than one, but a lot of Vibrio spp. (about 45%) did not possess any plasmid. Most of these plasmid various derivatives ranged from 2.4 kb-23 kb, especially two strains of V. mimicus and one strain of V. furnissii carried one high-molecular weight plasmid (molecular weight ranging between 70 kb-100 kb). Results of restriction analysis for plasmid of this three strains were by no means the rule. For detection of tdh and ctx gene, the virulence factor involved in the pathogenesis, we carried out the TDH, CT assay, PCR amplification, and hybridization. A total 11 strains were produced TDH, involved in 4 strains of V. parahaemolyticus and 1 strain of V. cholerae non-01 from clinical isolates and 6 strains of environmental isolates. Nine strains of 11 strains, involved in 4 strains of V. parahaemolyticus and 1 strain of V. cholerae non-01 from clinical isolates and 4 strains of V. parahaemolyticus from environmental isolates, could be successfully amplified in 400 bp by PCR, no amplification products were obtained from TDH-negative strains. The PCR results were consistent with DNA hybridization. In the experiments of ctx gene detection, in all, 3 strains of V. cholerae non-01 from clinical isolate and 1 strains of V. cholerae non-01 from environmental isolate were observed CT- positive. These CT-producing strains amplified in 302 bp by PCR for the detection of ctx gene. All CT-producing strains hybridized with digoxigenin-labeled DNA probe, while CT-negative strains did not hybridize. Also hybridization tests results for detection of ctx gene consistent with PCR.
Cholera ; Digestion ; DNA ; Plasmids ; Polymerase Chain Reaction ; Vibrio* ; Virulence Factors* ; Virulence*

No abstract available.
Escherichia coli O157* ; Escherichia coli* ; Escherichia* ; Polymerase Chain Reaction* ; Virulence Factors* ; Virulence*

In the present study, we investigated the differences in the levels of expression of virulence factors between blood isolates of Candida albicans and commensal strain isolated from the oral cavities of health volunteers, and correlations between virulence factors. Blood isolates of 33 and commenal isolates of 71 were characterized by putative virulence factors such as proteinase production (PROT), an ability to adhere to epithelial cells (ADH), cell surface hydrophobicity (CSH), phospholipase production (PLASE), and hyphal transition (GERM). In PROT, ADH, CSH, and PLASE, the means of expression of blood isolates were higher compared with those of commensal isolates, however statistical significance was only shown in CSH (p=0.036). On the contrary, mean expression of GERM of blood isolates was lower than that of commensal isolates. Of relationships between virulence factors, although a negative correlation of PROT with CSH was obtained, the correlation was relatively low (r=-0.316, p=0.001). These results suggest that higher expression of CSH is a more distinguishing character in virulent blood isolates of C. albicans and that the expression of virulence factors are independent.
Candida albicans* ; Candida* ; Epithelial Cells ; Healthy Volunteers* ; Hydrophobic and Hydrophilic Interactions ; Phospholipases ; Virulence Factors ; Virulence* ; Volunteers