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Title: Translocation of an 89-kDa periplasmic protein is associated with Holospora infection

Abstract

The symbiotic bacterium Holospora obtusa infects the macronucleus of the ciliate Paramecium caudatum. After ingestion by its host, an infectious form of Holospora with an electron-translucent tip passes through the host digestive vacuole and penetrates the macronuclear envelope with this tip. To investigate the underlying molecular mechanism of this process, we raised a monoclonal antibody against the tip-specific 89-kDa protein, sequenced this partially, and identified the corresponding complete gene. The deduced protein sequence carries two actin-binding motifs. Indirect immunofluorescence microscopy shows that during escape from the host digestive vacuole, the 89-kDa proteins translocates from the inside to the outside of the tip. When the bacterium invades the macronucleus, the 89-kDa protein is left behind at the entry point of the nuclear envelope. Transmission electron microscopy shows the formation of fine fibrous structures that co-localize with the antibody-labeled regions of the bacterium. Our findings suggest that the 89-kDa protein plays a role in Holospora's escape from the host digestive vacuole, the migration through the host cytoplasm, and the invasion into the macronucleus.

Authors:
 [1];  [2];  [3];  [3];  [1];  [4]
  1. Biological Institute, Faculty of Science, Yamaguchi University, Yoshida 1677-1, Yamaguchi 753-8512 (Japan)
  2. Institute for Genetic Research and Biotechnology, Shizuoka University, Ohya 836, Suruga-ku, Shizuoka 422-8529 (Japan)
  3. Universite de Montreal, Departement de Biochimie and Canadian Institute for Advanced Research, Program in Evolutionary Biology, Montreal, Que., Canada H3C 3J7 (Canada)
  4. Biological Institute, Faculty of Science, Yamaguchi University, Yoshida 1677-1, Yamaguchi 753-8512 (Japan). E-mail: fujishim@yamaguchi-u.ac.jp
Publication Date:
OSTI Identifier:
20713462
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 337; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2005.09.175; PII: S0006-291X(05)02178-9; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ACTIN; AMINO ACID SEQUENCE; BACTERIA; CYTOPLASM; GENES; INGESTION; MONOCLONAL ANTIBODIES; PARAMECIUM; TRANSLOCATION; TRANSMISSION ELECTRON MICROSCOPY

Citation Formats

Iwatani, Koichi, Dohra, Hideo, Lang, B. Franz, Burger, Gertraud, Hori, Manabu, and Fujishima, Masahiro. Translocation of an 89-kDa periplasmic protein is associated with Holospora infection. United States: N. p., 2005. Web. doi:10.1016/j.bbrc.2005.09.175.
Iwatani, Koichi, Dohra, Hideo, Lang, B. Franz, Burger, Gertraud, Hori, Manabu, & Fujishima, Masahiro. Translocation of an 89-kDa periplasmic protein is associated with Holospora infection. United States. doi:10.1016/j.bbrc.2005.09.175.
Iwatani, Koichi, Dohra, Hideo, Lang, B. Franz, Burger, Gertraud, Hori, Manabu, and Fujishima, Masahiro. Fri . "Translocation of an 89-kDa periplasmic protein is associated with Holospora infection". United States. doi:10.1016/j.bbrc.2005.09.175.
@article{osti_20713462,
title = {Translocation of an 89-kDa periplasmic protein is associated with Holospora infection},
author = {Iwatani, Koichi and Dohra, Hideo and Lang, B. Franz and Burger, Gertraud and Hori, Manabu and Fujishima, Masahiro},
abstractNote = {The symbiotic bacterium Holospora obtusa infects the macronucleus of the ciliate Paramecium caudatum. After ingestion by its host, an infectious form of Holospora with an electron-translucent tip passes through the host digestive vacuole and penetrates the macronuclear envelope with this tip. To investigate the underlying molecular mechanism of this process, we raised a monoclonal antibody against the tip-specific 89-kDa protein, sequenced this partially, and identified the corresponding complete gene. The deduced protein sequence carries two actin-binding motifs. Indirect immunofluorescence microscopy shows that during escape from the host digestive vacuole, the 89-kDa proteins translocates from the inside to the outside of the tip. When the bacterium invades the macronucleus, the 89-kDa protein is left behind at the entry point of the nuclear envelope. Transmission electron microscopy shows the formation of fine fibrous structures that co-localize with the antibody-labeled regions of the bacterium. Our findings suggest that the 89-kDa protein plays a role in Holospora's escape from the host digestive vacuole, the migration through the host cytoplasm, and the invasion into the macronucleus.},
doi = {10.1016/j.bbrc.2005.09.175},
journal = {Biochemical and Biophysical Research Communications},
number = 4,
volume = 337,
place = {United States},
year = {Fri Dec 02 00:00:00 EST 2005},
month = {Fri Dec 02 00:00:00 EST 2005}
}
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