Determination of crucial epitopes in the sperm protein calsperin employing synthetic peptides and monoclonal antibodies.

ABSTRACT: The chaperone protein calsperin is exclusively expressed in the testes and is essential for sperm migration from the uterus into the oviduct. During spermatogenesis, calsperin interacts with ADAM3, a spermatozoon membrane protein required for fertilization. In this study, we characterized a calsperin epitope by using two monoclonal antibodies and resin-bound calsperin peptides, which were tested for reactivity using a modified enzyme-linked immunosorbent assay. An epitope located at the C-terminal end of calsperin corresponding to amino acids ²²⁸ WEKHFLDAS²³⁷ was identified. Three hot spot amino acids were essential for antibody binding whereas the remaining amino acids in the identified epitope appeared to be essential for bringing the critical contact residues into

SUBMITTER: Bergmann AC 

PROVIDER: S-EPMC10078156 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature