Xyloglucan endotransglycosylase/hydrolase increases tightly-bound xyloglucan and chain number but decreases chain length contributing to the defense response that Glycine max has to Heterodera glycines

• Published in: PloS one 2021-01, Vol.16 (1), p.e0244305-e0244305
• Main Authors: Niraula, Prakash M, Zhang, Xuefeng, Jeremic, Dragica, Lawrence, Katherine S, Klink, Vincent P
• Format: Article
• Language: English
• Subjects: Animals; Biology and life sciences; Botanical research; Chromatography, Gel; Ecology and Environmental Sciences; Engineering and Technology; Female; Genotype; Glucans - chemistry; Glucans - metabolism; Glycine max - enzymology; Glycine max - genetics; Glycine max - parasitology; Glycosidases; Glycosyltransferases - antagonists & inhibitors; Glycosyltransferases - genetics; Glycosyltransferases - metabolism; Health aspects; Host-Parasite Interactions; Molecular Weight; Nematode diseases of plants; Physical Sciences; Physiological aspects; Plant Proteins - metabolism; Plant Roots - parasitology; Plants, Genetically Modified - enzymology; Plants, Genetically Modified - genetics; Principal Component Analysis; Research and Analysis Methods; RNA Interference; RNA, Small Interfering - metabolism; Tylenchida - physiology; Xylans - chemistry; Xylans - metabolism; Xyloglucans
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0244305

The Glycine max xyloglucan endotransglycosylase/hydrolase (EC 2.4.1.207), GmXTH43, has been identified through RNA sequencing of RNA isolated through laser microdissection of Heterodera glycines-parasitized root cells (syncytia) undergoing the process of defense. Experiments reveal that genetically increasing XTH43 transcript abundance in the H. glycines-susceptible genotype G. max[Williams 82/PI 518671] decreases parasitism. Experiments presented here show decreasing XTH43 transcript abundance through RNA interference (RNAi) in the H. glycines-resistant G. max[Peking/PI 548402] increases susceptibility, but it is unclear what role XTH43 performs. The experiments presented here show XTH43 overexpression decreases the relative length of xyloglucan (XyG) chains, however, there is an increase in the amount of those shorter chains. In contrast, XTH43 RNAi increases XyG chain length. The experiments show that XTH43 has the capability to function, when increased in its expression, to limit XyG chain extension. This outcome would likely impair the ability of the cell wall to expand. Consequently, XTH43 could provide an enzymatically-driven capability to the cell that would allow it to limit the ability of parasitic nematodes like H. glycines to develop a feeding structure that, otherwise, would facilitate parasitism. The experiments presented here provide experimentally-based proof that XTHs can function in ways that could be viewed as being able to limit the expansion of the cell wall.