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Human sperm TMEM95 binds eggs and facilitates membrane fusion.
Tang, Shaogeng; Lu, Yonggang; Skinner, Will M; Sanyal, Mrinmoy; Lishko, Polina V; Ikawa, Masahito; Kim, Peter S.
Afiliación
  • Tang S; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305.
  • Lu Y; Sarafan ChEM-H, Stanford University, Stanford, CA 94305.
  • Skinner WM; Immunology Frontier Research Center, Osaka University, Osaka 565-0871, Japan.
  • Sanyal M; Department of Experimental Genome Research, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan.
  • Lishko PV; Endocrinology Graduate Group, University of California, Berkeley, Berkeley, CA 94720.
  • Ikawa M; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305.
  • Kim PS; Sarafan ChEM-H, Stanford University, Stanford, CA 94305.
Proc Natl Acad Sci U S A ; 119(40): e2207805119, 2022 10 04.
Article en En | MEDLINE | ID: mdl-36161911
Tmem95 encodes a sperm acrosomal membrane protein, whose knockout has a male-specific sterility phenotype in mice. Tmem95 knockout murine sperm can bind to, but do not fuse with, eggs. How TMEM95 plays a role in membrane fusion of sperm and eggs has remained elusive. Here, we utilize a sperm penetration assay as a model system to investigate the function of human TMEM95. We show that human TMEM95 binds to hamster egg membranes, providing evidence for a TMEM95 receptor on eggs. Using X-ray crystallography, we reveal an evolutionarily conserved, positively charged region of TMEM95 as a putative receptor-binding surface. Amino acid substitutions within this region of TMEM95 ablate egg-binding activity. We identify monoclonal antibodies against TMEM95 that reduce the number of human sperm fused with hamster eggs in sperm penetration assays. Strikingly, these antibodies do not block binding of sperm to eggs. Taken together, these results provide strong evidence for a specific, receptor-mediated interaction of sperm TMEM95 with eggs and suggest that this interaction may have a role in facilitating membrane fusion during fertilization.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Óvulo / Interacciones Espermatozoide-Óvulo / Espermatozoides / Proteínas de Plasma Seminal / Infertilidad Masculina / Fusión de Membrana / Proteínas de la Membrana Límite: Animals / Humans / Male Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2022 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Óvulo / Interacciones Espermatozoide-Óvulo / Espermatozoides / Proteínas de Plasma Seminal / Infertilidad Masculina / Fusión de Membrana / Proteínas de la Membrana Límite: Animals / Humans / Male Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2022 Tipo del documento: Article Pais de publicación: Estados Unidos