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United States Department of Agriculture

Agricultural Research Service


item Witchell, Timothy
item Bulach, Dieter
item Hoke, David
item Driesen, Steve
item Stanton, Thaddeus
item Zuerner, Richard
item Cordwell, Stuart
item Adler, Ben

Submitted to: Australian Society for Microbiology
Publication Type: Abstract Only
Publication Acceptance Date: 5/1/2008
Publication Date: 7/6/2008
Citation: Witchell, T., Bulach, D., Hoke, D., Driesen, S., Stanton, T.B., Zuerner, R.L., Cordwell, S., Adler, B. 2008. Bhmp39 proteins of B. hyodysenteriae form high molecular weight complexes [abstract]. Australian Society for Microbiology. p.04.39.

Interpretive Summary:

Technical Abstract: Brachyspira hyodysenteriae is the aetiological agent of swine dysentery, a severe mucohaemorrhagic diarrhoeal disease of pigs, with economic significance for the global pork industry. The most abundant outer membrane proteins of B. hyodysenteriae are from the Bhmp39 family of proteins. Eight bhmp39 genes (bhmp39a-h) encoding highly similar, 39 kDa proteins have been identified by Southern blotting in the genome of B. hyodysenteriae strain B204. Of these, only bhmp39f and bhmp39h were found to be expressed. During this study, analysis of the near-complete genome sequence of a recent Victorian clinical isolate of B. hyodysenteriae (strain X576) has revealed that it contains only five of the previously published bhmp39 genes, along with two novel bhmp39-like genes. These two genes are also encoded by the B204 strain genome, according to a draft genome sequence. The function of proteins produced by these genes is currently unknown and the biological basis for maintaining these highly similar genes is unclear. Recently, we have observed that Bhmp39 proteins are present in the outer membrane of B. hyodysenteriae strain X576 in six multimeric complexes ranging in size from 60 to 115 kDa with an approximate 11 kDa size difference between each complex. These complexes are stable in 6M urea and in 2% SDS but are heat-labile. Mass spectrometry analysis of boiled samples demonstrated that both Bhmp39e and Bhmp39h proteins were present.

Last Modified: 06/24/2017
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