The PirB toxin protein from Vibrio parahaemolyticus induces apoptosis in hemocytes of Penaeus vannamei: PirB induces shrimp hemocytes apoptosis. Issue 1 (31st December 2021)
- Record Type:
- Journal Article
- Title:
- The PirB toxin protein from Vibrio parahaemolyticus induces apoptosis in hemocytes of Penaeus vannamei: PirB induces shrimp hemocytes apoptosis. Issue 1 (31st December 2021)
- Main Title:
- The PirB toxin protein from Vibrio parahaemolyticus induces apoptosis in hemocytes of Penaeus vannamei
- Authors:
- Zheng, Zhou
Li, Ruiwei
Aweya, Jude Juventus
Yao, Defu
Wang, Fan
Li, Shengkang
Tuan, Tran Ngoc
Zhang, Yueling - Abstract:
- ABSTRACT: Acute hepatopancreatic necrosis disease (AHPND) is a major debilitating disease that causes massive shrimp death resulting in substantial economic losses in shrimp aquaculture. The Pir toxin proteins secreted by a unique strain of Vibrio parahaemolyticus play an essential role in the pathogenesis of AHPND. At present, most studies on the effects of Pir toxin proteins in shrimp focus on digestive tissues or organs such as hepatopancreas, stomach, etc., with none on the immune organs. In the present study, two recombinant Pir toxin proteins (rPirA and rPirB) of V. parahaemolyticus were expressed with rPirB shown to enter shrimp hemocytes. Employing pull-down and LC-MS/MS analysis, GST-rPirB was found to interact with 13 proteins in hemocytes, including histone H3 and histone H4 and among which histone H4 had the highest protein score. Further analysis using GST pull-down and Far-Western blot analysis revealed that rPirB could interact with histone H4. In addition, using the purified nucleosome protein from Drosophila S2 cells, it was found that PirB protein could specifically bind to histones. When flow cytometry was applied, it was observed that the interaction between PirB and histones in shrimp hemocytes induces apoptosis, which results in the dephosphorylation of Serine 10 in histone H3. Collectively, the current study shows that in addition to its effect on the digestive tract of shrimp, the PirB toxin protein interacts with histones to affect theABSTRACT: Acute hepatopancreatic necrosis disease (AHPND) is a major debilitating disease that causes massive shrimp death resulting in substantial economic losses in shrimp aquaculture. The Pir toxin proteins secreted by a unique strain of Vibrio parahaemolyticus play an essential role in the pathogenesis of AHPND. At present, most studies on the effects of Pir toxin proteins in shrimp focus on digestive tissues or organs such as hepatopancreas, stomach, etc., with none on the immune organs. In the present study, two recombinant Pir toxin proteins (rPirA and rPirB) of V. parahaemolyticus were expressed with rPirB shown to enter shrimp hemocytes. Employing pull-down and LC-MS/MS analysis, GST-rPirB was found to interact with 13 proteins in hemocytes, including histone H3 and histone H4 and among which histone H4 had the highest protein score. Further analysis using GST pull-down and Far-Western blot analysis revealed that rPirB could interact with histone H4. In addition, using the purified nucleosome protein from Drosophila S2 cells, it was found that PirB protein could specifically bind to histones. When flow cytometry was applied, it was observed that the interaction between PirB and histones in shrimp hemocytes induces apoptosis, which results in the dephosphorylation of Serine 10 in histone H3. Collectively, the current study shows that in addition to its effect on the digestive tract of shrimp, the PirB toxin protein interacts with histones to affect the phosphorylation of histone H3-S10, thereby inducing apoptosis. … (more)
- Is Part Of:
- Virulence. Volume 12:Issue 1(2021)
- Journal:
- Virulence
- Issue:
- Volume 12:Issue 1(2021)
- Issue Display:
- Volume 12, Issue 1 (2021)
- Year:
- 2021
- Volume:
- 12
- Issue:
- 1
- Issue Sort Value:
- 2021-0012-0001-0000
- Page Start:
- 481
- Page End:
- 492
- Publication Date:
- 2021-12-31
- Subjects:
- Penaeus vannamei -- AHPND -- PirB -- hemocytes -- nucleosome proteins -- apoptosis -- dephosphorylation
Virulence (Microbiology) -- Periodicals
Bacterial diseases -- Periodicals
Molecular microbiology -- Periodicals
579.05 - Journal URLs:
- http://www.landesbioscience.com/journals/virulence ↗
http://www.tandfonline.com/toc/kvir20/current ↗
http://www.tandfonline.com/ ↗ - DOI:
- 10.1080/21505594.2021.1872171 ↗
- Languages:
- English
- ISSNs:
- 2150-5608
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25396.xml