Structural analysis of the flagellar capping protein FliD from Helicobacter pylori

So Yeon Cho; Wan Seok Song; Han-Byeol Oh; Han-Ul Kim; Hyun Suk Jung; Sung-Il Yoon

doi:10.1016/j.bbrc.2019.04.065

Structural analysis of the flagellar capping protein FliD from Helicobacter pylori

Biochem Biophys Res Commun. 2019 Jun 18;514(1):98-104. doi: 10.1016/j.bbrc.2019.04.065. Epub 2019 Apr 22.

Authors

So Yeon Cho¹, Wan Seok Song¹, Han-Byeol Oh¹, Han-Ul Kim², Hyun Suk Jung², Sung-Il Yoon³

Affiliations

¹ Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon, 24341, Republic of Korea.
² Department of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, 24341, Republic of Korea.
³ Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon, 24341, Republic of Korea; Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon, 24341, Republic of Korea. Electronic address: sungil@kangwon.ac.kr.

PMID: 31023530
DOI: 10.1016/j.bbrc.2019.04.065

Abstract

Helicobacter pylori is a pathogenic flagellated bacterium that infects the gastroduodenal mucosa and causes peptic ulcers in humans. FliD caps the distal end of the flagellar filament and is essential in filament growth. Moreover, FliD has been studied to diagnose and prevent H. pylori infection. Here, we report structure-based molecular studies of H. pylori FliD (hpFliD). A crystal structure of hpFliD at 2.6 Å resolution presents a four-domain (D2-D5) structure, where the D3 domain forms a central platform surrounded by the other three domains (D2, D4, and D5). hpFliD domains D2 and D3 structurally resemble those of FliD orthologs, whereas the D4 and D5 domains are exclusive to hpFliD. Moreover, our ELISA analysis using anti-H. pylori antibodies demonstrated that the hpFliD-specific D4 and D5 domains are highly antigenic compared to the D2 and D3 domains. Collectively, our structural and serological analyses underscore the structural role of hpFliD domains and provide a molecular basis for vaccine and diagnosis development.

Keywords: Crystal structure; Flagellum; FliD; Helicobacter pylori.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Crystallography, X-Ray
Flagella / chemistry*
Helicobacter Infections / microbiology*
Helicobacter pylori / chemistry*
Humans
Models, Molecular
Protein Conformation
Protein Domains

Substances

Bacterial Proteins
FlaD protein, Bacteria