Laboratory-confirmed case of yaws in a 10-year-old boy from the Republic of the Congo.

We report a case of yaws in a patient with puritic cutaneous eruption who was initially suspected of infection with monkeypox. The diagnosis was established by real-time PCR and sequencing of specific treponemal DNA sequences. This is the first report describing the use of DNA sequencing to identify Treponema pallidum subsp.

The sequence of the acidic repeat protein (arp) gene differentiates venereal from nonvenereal Treponema pallidum subspecies, and the gene has evolved under strong positive selection in the subspecies that causes syphilis.

Despite the completion of the Treponema pallidum genome project, only minor genetic differences have been found between the subspecies that cause venereal syphilis (ssp. pallidum) and the nonvenereal diseases yaws (ssp. pertenue) and bejel (ssp.

On the origin of the treponematoses: a phylogenetic approach.

Background: Since the first recorded epidemic of syphilis in 1495, controversy has surrounded the origins of the bacterium Treponema pallidum subsp. pallidum and its relationship to the pathogens responsible for the other treponemal diseases: yaws, endemic syphilis, and pinta. Some researchers have argued that the syphilis-causing bacterium, or its progenitor, was brought from the New World to Europe by Christopher Columbus and his men, while others maintain that the treponematoses, including syphilis, have a much longer history on the European continent.

Molecular characterization and analysis of a gene encoding the acidic repeat protein (Arp) of Treponema pallidum.

The acidic repeat protein (arp) genes from three subspecies of the treponeme Treponema pallidum (T. pallidum subsp. pallidum, Nichols strain; T.

Molecular cloning of a gene (poIA) coding for an unusual DNA polymerase I from Treponema pallidum.

The gene coding for the DNA polymerase I from Treponema pallidum, Nichols strain, was cloned and sequenced. Depending on which of the two alternative initiation codons was used, the protein was either 997 or 1015 amino acids long and the predicted protein had a molecular mass of either 112 or 114 kDa. Sequence comparisons with other polA genes showed that all three domains expected in the DNA polymerase I class of enzymes were present in the protein (5'-3' exonuclease, 3'-5' exonuclease and polymerase domains).