biostudies-literatureUnknown57Zhao SCystic echinococcosis (CE) is a zoonotic disease caused by the infection of Echinococcus granulosus (E. granulosus) larva. Currently, blocking the pathogenic cycle chain through immunoprophylaxis has become the main research direction. EgG1Y162 protein has good antigenicity and immunogenicity and is therefore a good candidate molecule for E. granulosus vaccine. Mature T cells express CTLA-4 on their surface, and its extracellular IgV region binds efficiently to the B7 molecules on antigen-presenting cells to deliver negative signals. We designed and prepared a recombinant vaccine by fusing CTLA-4IgV to the EgG1Y162 protein to exploit its binding properties. Bioinformatic methods were used to analyze the structure and epitopes of the proposed recombinant vaccine. The placement of 16 amino aBrazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicae13139https://www.ebi.ac.uk/biostudies/studies/S-EPMC11653501biostudies-literatureBioinformatic features and immunological response of recombinant antigen CTLA4-IgV-EgG1Y162 against Echinococcus granulosus.PMC11653501Zheng JLi YZhao SGong QCao CZhou WZhou YDing JZhou XKong HfalseBioinformatic features and immunological response of recombinant antigen CTLA4-IgV-EgG1Y162 against Echinococcus granulosus.Cystic echinococcosis (CE) is a zoonotic disease caused by the infection of Echinococcus granulosus (E. granulosus) larva. Currently, blocking the pathogenic cycle chain through immunoprophylaxis has become the main research direction. EgG1Y162 protein has good antigenicity and immunogenicity and is therefore a good candidate molecule for E. granulosus vaccine. Mature T cells express CTLA-4 on their surface, and its extracellular IgV region binds efficiently to the B7 molecules on antigen-presenting cells to deliver negative signals. We designed and prepared a recombinant vaccine by fusing CTLA-4IgV to the EgG1Y162 protein to exploit its binding properties. Bioinformatic methods were used to analyze the structure and epitopes of the proposed recombinant vaccine. The placement of 16 amino a2024-01-01T00:00:00Z20242026-06-14T05:27:06.078Z2026-06-14T03:08:19.596ZS-EPMC116535013960720110.1590/1414-431X2024e13139