Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine Bacterium Photobacterium sp. QA16

Lin Wei; Qingdong Zhang; Danrong Lu; Min Du; Xiangyu Xu; Wenshuang Wang; Yu-Zhong Zhang; Xunyi Yuan; Fuchuan Li

doi:10.3389/fmicb.2021.775124

Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine Bacterium Photobacterium sp. QA16

Front Microbiol. 2022 Jan 24:12:775124. doi: 10.3389/fmicb.2021.775124. eCollection 2021.

Authors

Lin Wei¹, Qingdong Zhang^{1

2}, Danrong Lu^{1

2}, Min Du¹, Xiangyu Xu¹, Wenshuang Wang¹, Yu-Zhong Zhang³, Xunyi Yuan⁴, Fuchuan Li¹

Affiliations

¹ National Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, Shandong University, Qingdao, China.
² School of Life Sciences and Technology, Weifang Medical University, Weifang, China.
³ College of Marine Life Sciences, Ocean University of China, Qingdao, China.
⁴ Department of General Surgery, Qilu Hospital (Qingdao), Cheeloo College of Medicine, Shandong University, Qingdao, China.

Abstract

Chondroitin sulfate (CS)/dermatan sulfate (DS) is a kind of sulfated polyanionic, linear polysaccharide belonging to glycosaminoglycan. CS/DS sulfatases, which specifically hydrolyze sulfate groups from CS/DS oligo-/polysaccharides, are potential tools for structural and functional studies of CD/DS. However, only a few sulfatases have been reported and characterized in detail to date. In this study, two CS/DS sulfatases, PB_3262 and PB_3285, were identified from the marine bacterium Photobacterium sp. QA16 and their action patterns were studied in detail. PB_3262 was characterized as a novel 4-O-endosulfatase that can effectively and specifically hydrolyze the 4-O-sulfate group of disaccharide GlcUAβ1-3GalNAc(4-O-sulfate) but not GlcUAβ1-3GalNAc(4,6-O-sulfate) and IdoUAα1-3GalNAc(4-O-sulfate) in CS/DS oligo-/polysaccharides, which is very different from the identified 4-O-endosulfatases in the substrate profile. In contrast, PB_3285 specifically hydrolyzes the 6-O-sulfate groups of GalNAc(6-O-sulfate) residues located at the reducing ends of the CS chains and is the first recombinantly expressed 6-O-exosulfatase to effectively act on CS oligosaccharides.

Keywords: chondroitin sulfate/dermatan sulfate; glycosaminoglycan; marine bacterium; substrate-degrading pattern; sulfatase.