Unraveling the Host-Selective Toxic Interaction of Cassiicolin with Lipid Membranes and Its Cytotoxicity

Phytopathology - Tập 112 Số 7 - Trang 1524-1536 - 2022
Kien Xuan Ngo1, Phuong Doan N. Nguyen2,1, Hirotoshi Furusho1, Makoto Miyata3, Tomomi Shimonaka3, Nguyễn Ngọc Bảo Châu4, Nguyen Phuong Vinh5, Nguyen Anh Nghia5, Tareg Omer Mohammed1, Takehiko Ichikawa1, Noriyuki Kodera1, Hiroki Konno1, Takeshi Fukuma1, Nguyễn Bảo Quốc6,2
1WPI Nano Life Science Institute, Kanazawa University, Kakuma-machi, Kanazawa, Japan
2Research Institute for Biotechnology and Environment, Nong Lam University, Ho Chi Minh City, Vietnam
3Department of Biology, Graduate School of Science, Osaka City University, Osaka, Japan
4Faculty of Biotechnology, Ho Chi Minh City Open University, Ho Chi Minh City, Vietnam
5Rubber Research Institute of Vietnam, Ho Chi Minh City, Vietnam
6Faculty of Biological Sciences, Nong Lam University, Ho Chi Minh City, Vietnam

Tóm tắt

Cassiicolin (Cas), a toxin produced by Corynespora cassiicola, is responsible for Corynespora leaf fall disease in susceptible rubber trees. Currently, the molecular mechanisms of the cytotoxicity of Cas and its host selectivity have not been fully elucidated. Here, we analyzed the binding of Cas1 and Cas2 to membranes consisting of different plant lipids and their membrane disruption activities. Using high-speed atomic force microscopy and confocal microscopy, we reveal that the binding and disruption activities of Cas1 and Cas2 on lipid membranes are strongly dependent on the specific plant lipids. The negative phospholipids, glycerolipids, and sterols are more sensitive to membrane damage caused by Cas1 and Cas2 than neutral phospholipids and betaine lipids. Mature Cas1 and Cas2 play an essential role in causing membrane disruption. Cytotoxicity tests on rubber leaves of Rubber Research Institute of Vietnam (RRIV) 1, RRIV 4, and Prang Besar (PB) 255 clones suggest that the toxins cause necrosis of rubber leaves, except for the strong resistance of PB 255 against Cas2. Cryogenic scanning electron microscopy analyses of necrotic leaf tissues treated with Cas1 confirm that cytoplasmic membranes are vulnerable to the toxin. Thus, the host selectivity of Cas toxin is attained by the lipid-dependent binding activity of Cas to the membrane, and the cytotoxicity of Cas arises from its ability to form biofilm-like structures and to disrupt specific membranes.

Từ khóa


Tài liệu tham khảo

10.1088/0957-4484/23/6/062001

10.1007/s12551-017-0356-5

10.1016/j.progsurf.2008.09.001

10.1146/annurev-biophys-083012-130324

10.1002/jmr.843

10.1007/BFb0114171

10.1039/dc9868100303

10.1016/S0955-0674(96)80021-4

10.3390/molecules25215110

10.1016/j.jmb.2006.11.086

10.1529/biophysj.107.126912

10.1007/s40858-021-00470-0

10.1016/j.jchromb.2006.10.051

10.1016/j.plantsci.2011.10.017

10.1016/j.funbio.2013.10.011

10.1007/s13225-012-0169-6

10.1016/0302-4598(88)80013-8

10.1094/PHYTO-99-9-1015

10.1016/S1360-1385(01)02216-6

10.1039/C9BM00134D

10.1007/s12154-008-0010-6

10.4161/psb.3.2.5051

10.1002/mame.201300285

10.1016/S1360-1385(98)01233-3

10.1016/j.sbi.2019.02.008

10.1006/abio.1995.1070

10.1007/s42464-020-00047-7

Kang J., 2011, Arab. B., 9, e0153, 10.1199/tab.0153

10.1038/nnano.2016.236

10.1128/JB.00160-16

10.1038/s41565-020-00798-9

10.1038/nature09450

10.1016/j.phytochem.2011.04.023

10.1038/s41467-019-14045-w

10.3389/fmicb.2018.00276

10.1104/pp.53.3.496

10.7554/eLife.64682

10.1146/annurev.arplant.59.032607.092734

10.1016/j.toxrep.2019.06.021

10.1104/pp.17.01573

10.1007/978-1-4939-8894-5_3

10.1007/s11046-008-9138-8

10.7554/eLife.04806

Ngo K. X., 2021, Bio-protocol.

Nguyen H. D., 2014, J. Rubber Res., 17, 187

10.1093/jmicro/dfl014

10.1016/0048-4059(76)90036-9

10.1016/j.fct.2017.12.047

10.1104/pp.58.4.595

10.1371/journal.pone.0254541

10.1016/j.fgb.2019.05.004

10.1002/19960401NT2

10.1016/j.cpb.2019.02.002

10.1038/s41467-017-01466-8

10.1371/journal.pone.0184908

10.1155/2013/152941

10.1094/PHYTO-12-17-0407-R

10.1111/nph.12754

10.1071/FP04135

10.1111/j.1574-6976.2012.00350.x

10.1126/science.1205510

10.1038/nprot.2012.047

10.1007/s12275-018-7497-5