Epitope topology and removal of mouse acrosomal plasma membrane by P12-targeted immunoaggregation

Han Jia Lin, Ching Wei Luo, Chia Yih Wang, Yee Hsiung Chen

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

P12 is a Kazal-type trypsin inhibitor that has been purified from mouse seminal vesicle secretion. We observed a slight impact of P12 on sperm capacitation, and demonstrated the removal of plasma membrane overlaying the acrosome region by immunoaggregation of P12 on mouse sperm. Further, we compared the immunoreactivity of P12 antibody to ten P12 variants, including six single-site mutated mutants (R19L, Y21V, D22G, R43G, K44S, and R45T), two multisite mutated mutants (R43G/K44S/R45T and L50H/R52G/K53A), and two deletion mutants (Nd10 and Cd8) in which 10 and 8 residues were deleted from the N- and C-terminals, respectively. We found that the N-terminal region, 43RKR45, and the C-terminal region, but not R19, Y21, and D22, are involved in the three epitopes that reside on one side and are three-dimensionally distant from R19, Y21, and D22 on the P12 molecule. Based on the epitope topology, we elucidated the structural basis by which P12 antibody immunoaggregated P12 on sperm head.

Original languageEnglish
Pages (from-to)284-288
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume349
Issue number1
DOIs
Publication statusPublished - 2006 Oct 13

Fingerprint

Cell membranes
Epitopes
Cell Membrane
Topology
Sperm Capacitation
Sperm Head
Acrosome
Trypsin Inhibitors
Antibodies
Seminal Vesicles
Spermatozoa
Molecules

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "P12 is a Kazal-type trypsin inhibitor that has been purified from mouse seminal vesicle secretion. We observed a slight impact of P12 on sperm capacitation, and demonstrated the removal of plasma membrane overlaying the acrosome region by immunoaggregation of P12 on mouse sperm. Further, we compared the immunoreactivity of P12 antibody to ten P12 variants, including six single-site mutated mutants (R19L, Y21V, D22G, R43G, K44S, and R45T), two multisite mutated mutants (R43G/K44S/R45T and L50H/R52G/K53A), and two deletion mutants (Nd10 and Cd8) in which 10 and 8 residues were deleted from the N- and C-terminals, respectively. We found that the N-terminal region, 43RKR45, and the C-terminal region, but not R19, Y21, and D22, are involved in the three epitopes that reside on one side and are three-dimensionally distant from R19, Y21, and D22 on the P12 molecule. Based on the epitope topology, we elucidated the structural basis by which P12 antibody immunoaggregated P12 on sperm head.",
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Epitope topology and removal of mouse acrosomal plasma membrane by P12-targeted immunoaggregation. / Lin, Han Jia; Luo, Ching Wei; Wang, Chia Yih; Chen, Yee Hsiung.

In: Biochemical and Biophysical Research Communications, Vol. 349, No. 1, 13.10.2006, p. 284-288.

Research output: Contribution to journalArticle

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