Title |
Comparative and bioinformatics analyses of pathogenic bacterial secretomes identified by mass spectrometry in Burkholderia species |
Author |
Thao Thi Nguyen1, Tae-Soo Chon2, Jaehan Kim3, Young-Su Seo1*, and Muyoung Heo4* |
Address |
1Department of Microbiology, Pusan National University, Busan 46241, Republic of Korea, 2Department of Biological Sciences, Pusan National University, Busan 46241, Republic of Korea, 3Department of Food and Nutrition, Chungnam National University, Daejeon 34134, Republic of Korea, 4Department of Physics, Pusan National University, Busan 46241, Republic of Korea |
Bibliography |
Journal of Microbiology, 55(7),568–582, 2017,
|
DOI |
10.1007/s12275-017-7085-0
|
Key Words |
Burkholderia glumae, Burkholderia gladioli, secretome,
NCSP, sequence analysis |
Abstract |
Secreted proteins (secretomes) play crucial roles during
bacterial pathogenesis in both plant and human hosts. The
identification and characterization of secretomes in the two
plant pathogens Burkholderia glumae BGR1 and B. gladioli
BSR3, which cause diseases in rice such as seedling blight,
panicle blight, and grain rot, are important steps to not only
understand the disease-causing mechanisms but also find
remedies for the diseases. Here, we identified two datasets of
secretomes in B. glumae BGR1 and B. gladioli BSR3, which
consist of 118 and 111 proteins, respectively, using mass spectrometry
approach and literature curation. Next, we characterized
the functional properties, potential secretion pathways
and sequence information properties of secretomes of
two plant pathogens in a comparative analysis by various computational
approaches. The ratio of potential non-classically
secreted proteins (NCSPs) to classically secreted proteins
(CSPs) in B. glumae BGR1 was greater than that in B. gladioli
BSR3. For CSPs, the putative hydrophobic regions (PHRs)
which are essential for secretion process of CSPs were screened
in detail at their N-terminal sequences using hidden Markov
model (HMM) – based method. Total 31 pairs of homologous
proteins in two bacterial secretomes were indicated
based on the global alignment (identity ≥ 70%). Our results
may facilitate the understanding of the species-specific features
of secretomes in two plant pathogenic Burkholderia
species. |