Journal
FRONTIERS IN CELLULAR AND INFECTION MICROBIOLOGY
Volume 10, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fcimb.2020.603457
Keywords
Brucella; T4SS; effector; BspF; lysine crotonylation; crotonyltransferase
Categories
Funding
- National Key Research and Development Program Projects of China [2017YFD0500901]
- National Science Foundation for Young Scientists of China [31702276]
- National Key Program for Infectious Disease of China [2018ZX10101002-002]
- State Key Program of National Natural Science of China [U1808202]
- Major science and technology projects of Inner Mongolia of China
- NSFC International (regional) cooperation and exchange program [31961143024]
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The study revealed that BspF can affect the crotonylation level of host proteins, thereby promoting the intracellular survival and replication of Brucella.
In Brucella spp., the type IV secretion system (T4SS) is essential for bacterial intracellular survival and inhibition of the host innate immune response. The Brucella T4SS secretes 15 different effectors to escape host immunity and promote intracellular replication. Among them, BspF has a GNAT-family acetyltransferase domain, implying its acetyltransferase activity. We confirmed that BspF has acetyltransferase activity (data not shown) and de-crotonyltransferase activity. However, BspF overexpressed in HEK-293T cells can also enhance octamer crotonylation in vitro. Then we enriched crotonylated proteins and conducted LC-MS to study the crotonylation changes of proteins in HEK-293T cells caused by BspF overexpression. A total of 5,559 crotonylation sites were identified on 1,525 different proteins, of which 331 sites on 265 proteins were significantly changed. We found that Rab9A and RAP1B in proteomics data have a great impact on Brucella survival, so we speculate that BspF may influence the function of host proteins by altering crotonylation, thereby promoting the intracellular propagation of Brucella.
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