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Title: PROTEOMICS TECHNOLOGY FOR IDENTIFICATION OF HAEMOPHILUS PARASUIS PROTEINS FOR VACCINE DEVELOPMENT (ORAL PRESENTATION FOR THE 82ND CONFERENCE OF RESEARCH WORKERS IN ANIMAL DISEASE)

Author
item TABATABAI, LOUISA

Submitted to: Research Workers in Animal Diseases Conference Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 9/21/2001
Publication Date: 11/10/2001
Citation: TABATABAI, L.B. PROTEOMICS TECHNOLOGY FOR IDENTIFICATION OF HAEMOPHILUS PARASUIS PROTEINS FOR VACCINE DEVELOPMENT (ORAL PRESENTATION FOR THE 82ND CONFERENCE OF RESEARCH WORKERS IN ANIMAL DISEASE). RESEARCH WORKERS IN ANIMAL DISEASES CONFERENCE PROCEEDINGS. 2001. Abstract #2.

Interpretive Summary:

Technical Abstract: Haemophilus parasuis is the causative agent of Glasser's disease of swine and comprises 15 serovars. Serovars 4, 5, 13 and 14 are prevalent in North America. Of the 15 serovars, six (serovars 1, 5, 10, 12, 13, and 14) are highly virulent, four (serovars 2, 4, 8, and 15) are less virulent and cause clinical symptoms without death, and five (serovars 3, 6, 7, 9, and 11) cause no clinical symptoms or lesions. H. parasuis is considered to b a re-emerging disease of swine raised in the high health status herds and segregated early weaning (SEW) swine production facilities. Commercial vaccines are available, but are not always efficacious. In order to identify potential subunit vaccine candidates, a study was undertaken to analyze systematically protein expression of H. parasuis using proteomics (two-dimensional electrophoresis followed by mass spectrometry). Proteins identified by proteomics and Western blots prepared from 2-D gels using sera from infected swine were analyzed using the PD-Quest 2-D analysis program. Major proteins were selected, digested with trypsin and analyzed by MALDI-TOF mass spectrometry and matched to the H influenzae and other SwissProt databases. Sixty of the 348 annotated protein spots were selected for further analysis, and four of these were identified thus far.