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

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

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

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

Some transcriptional regulators contribute to the expression of Streptococcus mutans (S. mutans) cariogenic virulence factors. Although the target sequence transcriptional regulators anchored on the cell wall and the molecular mechanism of the regulation of S. mutans are yet to be clarified, certain global regulators potentially associated with the cariogenicity of S. mutans have been identified. This review is about these related transcriptional regulators, their function, and possible mechanisms.
Gene Expression Regulation, Bacterial ; Myocarditis ; Streptococcal Infections ; Streptococcus mutans ; Transcription, Genetic ; Virulence ; Virulence Factors