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A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
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Published on: July 31, 2012

Type-II major-surface-glycoprotein family of Pneumocystis carinii under the control of novel expression elements

M Wada1, Y Nakamura

  • 1Department of Tumor Biology, The Institute of Medical Science, The University of Tokyo, Japan.

DNA Research : an International Journal for Rapid Publication of Reports on Genes and Genomes
|September 24, 1999
PubMed

Insights

Pneumocystis carinii major surface glycoproteins (MSGs) utilize a novel type-II expression site, distinct from the previously known type-I, for antigenic variation. This study details the characteristics of type-II UCS elements and their associated MSG gene family.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Immunology

Background:

  • Pneumocystis carinii possesses abundant major surface glycoproteins (MSGs) crucial for antigenic variation.
  • MSG gene expression is typically regulated by a unique type-I upstream coordinating sequence (UCS).
  • Previous work suggested the existence of alternative UCS elements, termed type-II UCS.

Purpose of the Study:

  • To characterize the features of type-II UCS elements.
  • To identify and analyze MSG genes controlled by type-II UCS (type-II MSG family).
  • To understand the structural conservation of type-II MSGs.

Main Methods:

  • cDNA analysis
  • Genomic analysis
  • Antibody-based detection of proteins

Main Results:

  • Type-II UCS elements are found on most P. carinii chromosomes and are directly linked to type-II MSG genes.
  • Type-II MSG genes comprise two subtypes (2.3 kb and 3.3 kb).
  • Antibody detection revealed type-II UCS polypeptide products between 90-100 kDa.
  • Type-II MSG proteins conserve cysteine residues, similar to type-I MSGs, indicating structural importance.

Conclusions:

  • Pneumocystis carinii employs a distinct type-II UCS system for MSG gene expression and antigenic variation.
  • The type-II MSG family exhibits conserved cysteine residues, essential for structural integrity on the cell surface.
  • This discovery expands our understanding of P. carinii immune evasion mechanisms.

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