Evidence map›Paper›PMID 41808143›Full record

ArticleBMC veterinary research2026

Molecular characterization of Eimeria necatrix surface antigen SAG8 and SAG36 genes and their immunoprotective efficacy in chicken.

Feiyan Wang, Chi Zhang, Yongcui Feng, Danli Yan, Dandan Liu, Shijie Su, Zhaofeng Hou, Jinjun Xu, Jianping Tao

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Article in BMC veterinary research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Feiyan Wang *College of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Chi Zhang *College of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Yongcui FengCollege of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Danli YanCollege of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Dandan LiuCollege of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Shijie SuCollege of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Zhaofeng HouCollege of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Jinjun XuCollege of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China.
Jianping TaoCollege of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, Jiangsu, 225009, People's Republic of China. jptao@yzu.edu.cn.

Funding

National Natural Science Foundation of China No.31602039National Natural Science Foundation of China No. 31972698the 111 Project D18007 the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)the Key Research and Development Program of Jiangsu Province Modern Agriculture, BE2021354
6 · The paper itself

Abstract

backgroundSurface antigens (SAGs) are a class of membrane proteins anchored to the parasite surface via glycosylphosphatidylinositol (GPI) anchors. These antigens play critical roles in parasite adhesion and host cell invasion. However, studies on SAGs from Eimeria necatrix remain limited.

resultsIn this study, two sag genes, which exhibit differential expression in SZ and MZ-2 stages of E. necatrix, were cloned and expressed. The Ensag8 (XM_013584257.1) and Ensag36 (XM_013577436.1) genes, encoding proteins of 263 and 265 amino acids with predicted molecular weights of 27.83 kDa and 28.66 kDa, respectively. Bioinformatic analysis indicated that neither protein contains transmembrane domains, and phylogenetic classification placed both within the SAGA sub-family, with EnSAG8 showing close evolutionary proximity to EtSAG8. Recombinant proteins rEnSAG8 and rEnSAG36 were expressed predominantly as inclusion bodies in Escherichia coli, with apparent molecular weights of approximately 32 kDa and 36 kDa, respectively. Both rEnSAG8 and rEnSAG36 were recognized by a mouse anti-His tag monoclonal antibody and by convalescent serum from chickens infected with E. necatrix and E. tenella. The native EnSAG8 protein was detected in MZ-2 with an observed molecular weight of ~ 35 kDa, and EnSAG36 was detected in both SZ and MZ-2 at ~ 36 kDa. Immunolocalization analysis revealed that both native proteins are localized on the membranes of SZ and MZ-2. Transcriptional analysis indicated that Ensag8 is more highly expressed in MZ-2 than in SZ, whereas Ensag36 shows higher transcriptional levels in SZ than in MZ-2. Following the E. necatrix challenge, the anticoccidial index (ACI) of both the rEnSAG8- and rEnSAG36-immunized groups exceeded 160 at an immunization dose of 100 µg per chicken per immunization, with the rEnSAG8 group achieving a higher ACI than the rEnSAG36 group. Combined immunization with rEnSAG8 and rEnSAG36 conferred greater protection than immunization with either antigen alone.

conclusionsThis study provides insights into the characterization of SAGs from E. necatrix. The differential expression of Ensag8 and Ensag36 highlights their potential roles in different parasite stages. Immunization with these recombinant proteins demonstrated significant anticoccidial protection, with combined immunization offering the best results.

Indexed as

Antigens, ProtozoanAntigens, SurfaceChickensCoccidiosisEimeriaPoultry DiseasesProtozoan VaccinesAmino Acid SequenceAnimalsCloning, MolecularPhylogenyAntigens, ProtozoanAntigens, SurfaceProtozoan VaccinesEimeria necatrixGPI-anchored proteinImmunoprotectionProkaryotic expressionSAG proteinSubunit vaccine

Identifiers

PMID41808143
PMCPMC13088589

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.