Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-4-29
pubmed:databankReference
pubmed:abstractText
Four Streptococcus pneumoniae genes, phtA, phtB, phtD, and phtE, as well as the slr gene of group A streptococci (GAS), encode proteins with a histidine triad motif (HxxHxH). Pht proteins function as protective antigens against S. pneumoniae infection. A search of the GAS genome database identified a novel protein, HtpA, possessing five histidine triad motifs. The htpA gene was shown to encode a 92.5-kDa protein located downstream of the fbaA and lbp genes, while Western blot analyses revealed that HtpA protein was expressed on the cell surfaces of all group A, B, C, and G streptococcal isolates tested. Immunization of mice with rHtpA induced antigen-specific antibody production and was effective after a single immunization, with antibody titers remaining constant for at least 84days. In addition, HtpA-immunized mice survived after challenge with GAS strains isolated from patients with streptococcal toxic shock syndrome for significantly longer periods than sham-immunized mice. In that experiment, the HtpA-specific antibody was effectively induced by a single immunization and the specific antibody titer remained constant for at least 84days. These results indicate that the novel histidine triad protein HtpA is a candidate vaccine for GAS infection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1286-4579
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
414-23
pubmed:meshHeading
pubmed-meshheading:18403236-Animals, pubmed-meshheading:18403236-Antibodies, Bacterial, pubmed-meshheading:18403236-Antigens, Bacterial, pubmed-meshheading:18403236-Antigens, Surface, pubmed-meshheading:18403236-Blotting, Western, pubmed-meshheading:18403236-DNA, Bacterial, pubmed-meshheading:18403236-Female, pubmed-meshheading:18403236-Gene Order, pubmed-meshheading:18403236-Humans, pubmed-meshheading:18403236-Hydrolases, pubmed-meshheading:18403236-Mice, pubmed-meshheading:18403236-Mice, Inbred BALB C, pubmed-meshheading:18403236-Molecular Sequence Data, pubmed-meshheading:18403236-Molecular Weight, pubmed-meshheading:18403236-Sequence Analysis, DNA, pubmed-meshheading:18403236-Shock, Septic, pubmed-meshheading:18403236-Streptococcal Infections, pubmed-meshheading:18403236-Streptococcal Vaccines, pubmed-meshheading:18403236-Streptococcus pyogenes, pubmed-meshheading:18403236-Survival Analysis
pubmed:year
2008
pubmed:articleTitle
Molecular and biological characterization of histidine triad protein in group A streptococci.
pubmed:affiliation
Department of Oral and Molecular Microbiology, Osaka University Graduate School of Dentistry, 1-8 Yamadaoka, Suita, Osaka 565-0871, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't