Screening and Preliminary Identification of Inhibin α Subunit-Specific Nanobodies Through High-Throughput Sequencing Combined with Mass Spectrometry.

Jifu Ma, Zhumanov Kairat, Bupebayeva Lyalla, Zhongmei Ma, Wurelihazi Hazihan

Abstract read

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Article in Animals : an open access journal from MDPI, 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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5 · Who and what money

Authors and funding

5 authors.

Jifu MaCollege of Animal Science and Technology, Shihezi University, Shihezi 832003, China.

Zhumanov KairatCollege of Animal Science and Technology, Shihezi University, Shihezi 832003, China.

Bupebayeva LyallaDepartment of Microbiology, Virology and Immunology, Faculty of Veterinary Medicine, Kazakh National Agrarian Research University, Almaty 050010, Kazakhstan.

Zhongmei MaCollege of Animal Science and Technology, Shihezi University, Shihezi 832003, China.

Wurelihazi HazihanCollege of Animal Science and Technology, Shihezi University, Shihezi 832003, China.

Funding

National Natural Science Foundation of China 31960709

6 · The paper itself

Abstract

Inhibin, a water-soluble protein emitted by the gonads, plays a pivotal role in regulating the release of follicle-stimulating hormone (FSH) from the pituitary gland, which, in turn, influences follicular growth, gamete production, and the secretion of associated hormones. We performed high-throughput sequencing of the nanobody gene in the lymphocytes of Bactrian camels before and after inhibin α protein immunization followed by mass spectrometry analysis of specific antibodies to this protein in the serum following immunization to screen for inhibin α subunit-specific nanobodies. Seven inhibin α-specific nanobodies, namely Nb-1712, Nb-1971, Nb-2000, Nb-799, Nb-2004, Nb-1737, and Nb-338, were identified through high-throughput sequencing and mass spectrometry. Following the construction and expression of a prokaryotic expression vector, five of these nanobody proteins were successfully produced. These proteins demonstrated high affinity for inhibin α in the indirect enzyme-linked immunosorbent assay. Notably, nanobodies Nb-1737, Nb-1971, and Nb-2004 significantly downregulated

Indexed as

FSHinhibin αnanobody

Identifiers

PMID42450668

DOI10.3390/ani16131961

PMCPMC13360298

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