Demonstration of antigenic and specific outer membrane protein(s) of Acinetobacter baumannii

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Date
2009-06
Authors
A.H.M. Shafiqul Islam
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Abstract
Acinetobacter baumannii has been recognized as an emerging nosocomial pathogen and is very often multi-resistant to antibiotics. It has also been identified as an important cause of morbidity and mortality in hospitals, especially among immunocompromised patients. Early diagnosis of infection caused by A. baumannii is the major strategy for controlling the nosocomial infection caused by this pathogen. Current identification of this bacteria is by conventional culture method and biochemical tests, which takes about 2 to 7 days to produce results. Hence, there is a need for a new rapid, sensitive, specific and economical test that would allow rapid management of A. baumannii infections. Development of a specific and sensitive diagnostic test requires a biomarker, which does not cross react with other bacteria and is specific only to A. baumannii. This formed the aim of this study; to detect the presence of a specific and antigenic biomarker for A. haumannii from the OMPs, which can be used for the development of a rapid and specific diagnostic test. Protein profiles of OMP lysates from the ATCC strain and clinical isolates of A. baumannii were demonstrated using the technique of SDS-PAGE and the protein profiles were compared. The protein profiles of the clinical isolates were 90% identical to that of the ATCC strain. Following this, the protein electrophoretograms were subjected to \\'estern blot analysis using serum from patients infected with A. haumannii and non-A. baumannii. The Western blot analysis revealed a 34.4 kDa antigen which was immunogenic when probed IgA, IgM and IgG of A. baumannii sera but did not cross react with sera from other nosocomial infections and normal controls. This was confirmed by repeated testing. Studies were also done to asses the effect of temperature on the expression of the OMPs. The OMPs profile expressed at 41°C showed few proteins were over-expressed (17.3, 22.4 and 60.5 kDa) while some proteins were down-regulated, suggesting that elevated body temperature during A. baumannii infection influences the expression of the bacterial proteins for survival of this bacterium. Further characterization ofthe 34.4 kDa protein demonstrated that it was associated with both OMPs and SAPs of A. baumannii and is not a glycoprotein. The 34.4 kDa antigen was present in all the clinical isolates of A. baumannii. The expression of this protein was enhanced in most cases suggesting that tl iis protein could also be related to the virulence of the bacteria. To date, no previous report is available with reference to this specific protein for A. baumannii. The results are encouraging in that the 34.4 kDa protein identified is specific for A. baumannii and can be used as a biomarker for development of a diagnostic test which would be faster and more specific than the current techniques of diagnosis. However, further studies need to be done to measure the antibody level against this specific protein, the sensitivity and specificity of the protein and the retention time of the antibody detectable in the serum of the infected patients.
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Keywords
Acinetobacter baumannii , Multi-resistant to antibiotics.
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