ORIGINAL RESEARCH article
Front. Immunol.
Sec. Vaccines and Molecular Therapeutics
This article is part of the Research TopicInnovative Vaccine Development Strategies for Parasitic DiseasesView all 6 articles
Site-and Structure-Specific Characterization of Glycoproteins of H11: Potent Vaccine Candidates against Parasitic Worm Haemonchus
Provisionally accepted
- 1Huazhong Agricultural University, Wuhan, China
- 2Shanghai Jiao Tong University, Shanghai, China
- 3BITS Pilani - Hyderabad Campus, Hyderabad, India
Select one of your emails
You have multiple emails registered with Frontiers:
Notify me on publication
Please enter your email address:
If you already have an account, please login
You don't have a Frontiers account ? You can register here
Parasitic worm (helminth) infections pose significant threats to global health and livestock productivity. Although mass spectrometry (MS)-based glycomics have revealed that helminths express structurally complex N-glycans, site- and structure-specific characterization of intact glycopeptides remains a major challenge. Here we employed advanced MS-based intact glycoproteomics to explore the N-glycosylation profile of H11 antigen – an important vaccine antigen derived from the pathogenic parasite Haemonchus contortus. We identified seven glycosylated aminopeptidases carrying 19 N-glycosylation sites with 31 distinct N-glycan structures. Notably, 13 N-glycopeptides were significantly enriched by H11-induced protective IgG antibodies. Our results revealed extensive structural heterogeneity and abundant core fucosylation among the identified N-glycopeptides. Additionally, molecular docking analyses demonstrated that these IgG-recognized N-glycopeptides were located on the protein surface or near substrate-access channels, indicating their potential as antigenic epitopes. Overall, this work provides a precise glycoproteomic characterization of a key helminth antigen and offers valuable insights for the rational design of vaccines against H. contortus and other related parasitic species.
Keywords: Parasitic worm, N-glycoproteome, intact N-glycopeptide analysis, Vaccine, glycan analysis
Received: 19 Jul 2025; Accepted: 03 Dec 2025.
Copyright: © 2025 Liu, Liu, Liu, Ye, Zhang, Peng, Gupta, Hu and WANG. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: CHUNQUN WANG
Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.