[Charactierization of a new antibacterial polypeptide isolated from human cervical mucas]

Sichuan Da Xue Xue Bao Yi Xue Ban. 2005 May;36(3):315-7.
[Article in Chinese]

Abstract

Objective: To identify a new antibactrial polypeptide HCP-1 isolated from human cervical mucus.

Methods: HCP-1 was isolated and purified from human cervical mucus, and N-terminal sequence of HCP-1 was determined. A degenerate primer was designed according to CodeHop methods, and an "anchor-oliga-dT primer" was used for the synthesis of cDNA. Using the degenerate primer and anchor-primer, cDNAs were amplified by PCR. The PCR products were cloned, sequenced, and analyzed by biological software.

Results: N-terminat sequence of HCP-1 was PKRKAEGDAK. The full length of HCP-1 cDNA was isolated and of which the sequence was the same as HMG-17. OMIGA software analysis indicated that this molecule contained an alpha-helix region.

Conclusion: The new antibacterial polypeptide isolated from human cervical mucus is HMG-17. It may play a role in the human cervical mucus and the alpha-helix domain may be its antibacterial activity region.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / isolation & purification*
  • Anti-Bacterial Agents / pharmacology*
  • Cervix Mucus / chemistry*
  • Cervix Mucus / physiology
  • Female
  • Humans
  • Peptides / chemistry
  • Peptides / isolation & purification
  • Peptides / pharmacology
  • Protein-Arginine N-Methyltransferases / chemistry
  • Protein-Arginine N-Methyltransferases / isolation & purification*
  • Protein-Arginine N-Methyltransferases / pharmacology*
  • Repressor Proteins / chemistry
  • Repressor Proteins / isolation & purification*
  • Repressor Proteins / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Peptides
  • Repressor Proteins
  • PRMT1 protein, human
  • Protein-Arginine N-Methyltransferases