Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-5-13
pubmed:databankReference
pubmed:abstractText
Wolbachia are intracellular alpha-proteobacteria, closely related to Rickettsia, that infect various arthropods and filarial parasites. In the present study, the cDNA encoding the aspartate aminotransferase (AspAT) of Wolbachia from the human pathogenic filarial parasite Onchocerca volvulus (Ov-WolAspAT) was identified. At the amino acid level, the identity of the Ov-WolAspAT was 56% to Rickettsia prowazekii AspAT and 54% to the AspAT of the nitrogen-fixing bacterium Sinorhizobium meliloti, but the highest degree of identity was found to the putative AspAT of Wolbachia from Brugia malayi and Drosophila melanogaster (85%). All of these bacterial AspATs are members of the AspAT subclass Ib. A 35 kDa fragment of the Ov-WolAspAT was expressed in Escherichia coli, and immunolocalization using polyclonal antibodies against this antigen revealed that Ov-WolAspAT is present in a considerable proportion of the Wolbachia from O. volvulus, as well as in the endobacteria of several other filarial parasites. Western blot analysis using recombinant Ov-WolAspAT as antigen showed that IgG1 antibodies were present in 70 (51%) individuals living in areas endemic for O. volvulus, B. malayi or Wuchereria bancrofti and no IgG4 or IgE antibodies were found. Among 40 sera of persons from Uganda and Liberia who were putatively not infected with human filarial parasites, 11 (28%) individuals presented IgG1 antibodies, while none of the 33 sera from healthy Europeans and none of the 14 sera from patients with proven Rickettsia or Brucella infections reacted with the antigen. These results also show that an intracellular protein of Wolbachia endobacteria (WolAspAT) acts as antigen in human filariasis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0932-0113
pubmed:author
pubmed:issnType
Print
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
38-47
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12743802-Amino Acid Sequence, pubmed-meshheading:12743802-Animals, pubmed-meshheading:12743802-Antibodies, Bacterial, pubmed-meshheading:12743802-Aspartate Aminotransferases, pubmed-meshheading:12743802-DNA, Bacterial, pubmed-meshheading:12743802-Endemic Diseases, pubmed-meshheading:12743802-Female, pubmed-meshheading:12743802-Humans, pubmed-meshheading:12743802-Immunoglobulin G, pubmed-meshheading:12743802-Immunohistochemistry, pubmed-meshheading:12743802-Molecular Sequence Data, pubmed-meshheading:12743802-Onchocerca volvulus, pubmed-meshheading:12743802-Onchocerciasis, pubmed-meshheading:12743802-Rabbits, pubmed-meshheading:12743802-Sequence Alignment, pubmed-meshheading:12743802-Seroepidemiologic Studies, pubmed-meshheading:12743802-Staining and Labeling, pubmed-meshheading:12743802-Wolbachia
pubmed:year
2003
pubmed:articleTitle
An aspartate aminotransferase of Wolbachia endobacteria from Onchocerca volvulus is recognized by IgG1 antibodies from residents of endemic areas.
pubmed:affiliation
Molecular Parasitology Section, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Strasse 74, 20359 Hamburg, Germany. Pfischer@bni.uni-hamburg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't