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Uptake and intracellular transportation of a bacterial surface protein in lymphoid cells.

Frick, Inga-Maria LU ; Axcrona, Karol; Härdig, Ylva; Tapper, Hans LU ; Gustafsson, Lotta LU ; Kellner, Roland; Leanderson, Tomas LU and Björck, Lars LU (2002) In Molecular Microbiology 44(4). p.917-934
Abstract
Some strains of the human pathogen Streptococcus pyogenes express a surface protein called protein H, which is released from the streptococcal surface by a cysteine proteinase produced by the bacteria. Here, we find that soluble protein H binds to the surface of lymphocytes and granulocytes, and that the molecule is taken up by lymphocytes and transported to the perinuclear region. The translocation over the cell membrane is rapid, and the uptake and intracellular transportation is not dependent on actin polymerization. Protein H could be immunoprecipitated from cell extracts and nuclear preparations of lymphocytes, and analysis of molecular interactions between pro-tein H and proteins of different cellular compart-ments demonstrated a... (More)
Some strains of the human pathogen Streptococcus pyogenes express a surface protein called protein H, which is released from the streptococcal surface by a cysteine proteinase produced by the bacteria. Here, we find that soluble protein H binds to the surface of lymphocytes and granulocytes, and that the molecule is taken up by lymphocytes and transported to the perinuclear region. The translocation over the cell membrane is rapid, and the uptake and intracellular transportation is not dependent on actin polymerization. Protein H could be immunoprecipitated from cell extracts and nuclear preparations of lymphocytes, and analysis of molecular interactions between pro-tein H and proteins of different cellular compart-ments demonstrated a binding to nucleophosmin/ B23, a protein known to shuttle between the cytoplasm and the nucleus, and to the nuclear proteins SET and hnRNP A2/B1. Nucleophosmin/B23 was co-immunoprecipitated with protein H from cell and nuclear extracts, and binding experiments, including kinetic analyses, suggest that protein H dissociating from nucleophosmin/B23 complexes in the perinuclear region or in the nucleus binds to proteins SET and hnRNP A2/B1. Finally, the uptake and intracellular transportation of protein H was found to result in a cytostatic effect on B and T lymphocytes. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
44
issue
4
pages
917 - 934
publisher
Wiley-Blackwell
external identifiers
  • pmid:12010489
  • wos:000175531300003
  • scopus:0036091005
ISSN
1365-2958
DOI
10.1046/j.1365-2958.2002.02931.x
language
English
LU publication?
yes
id
004b67da-98aa-4123-9427-12e0293266ab (old id 108242)
alternative location
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12010489&dopt=Abstract
date added to LUP
2007-07-04 15:57:14
date last changed
2017-01-01 05:16:45
@article{004b67da-98aa-4123-9427-12e0293266ab,
  abstract     = {Some strains of the human pathogen Streptococcus pyogenes express a surface protein called protein H, which is released from the streptococcal surface by a cysteine proteinase produced by the bacteria. Here, we find that soluble protein H binds to the surface of lymphocytes and granulocytes, and that the molecule is taken up by lymphocytes and transported to the perinuclear region. The translocation over the cell membrane is rapid, and the uptake and intracellular transportation is not dependent on actin polymerization. Protein H could be immunoprecipitated from cell extracts and nuclear preparations of lymphocytes, and analysis of molecular interactions between pro-tein H and proteins of different cellular compart-ments demonstrated a binding to nucleophosmin/ B23, a protein known to shuttle between the cytoplasm and the nucleus, and to the nuclear proteins SET and hnRNP A2/B1. Nucleophosmin/B23 was co-immunoprecipitated with protein H from cell and nuclear extracts, and binding experiments, including kinetic analyses, suggest that protein H dissociating from nucleophosmin/B23 complexes in the perinuclear region or in the nucleus binds to proteins SET and hnRNP A2/B1. Finally, the uptake and intracellular transportation of protein H was found to result in a cytostatic effect on B and T lymphocytes.},
  author       = {Frick, Inga-Maria and Axcrona, Karol and Härdig, Ylva and Tapper, Hans and Gustafsson, Lotta and Kellner, Roland and Leanderson, Tomas and Björck, Lars},
  issn         = {1365-2958},
  language     = {eng},
  number       = {4},
  pages        = {917--934},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {Uptake and intracellular transportation of a bacterial surface protein in lymphoid cells.},
  url          = {http://dx.doi.org/10.1046/j.1365-2958.2002.02931.x},
  volume       = {44},
  year         = {2002},
}