Bradyzoite development in Toxoplasma gondii and the hsp70 stress response

Louis M. Weiss, Yan Fen Ma, Peter M. Takvorian, Herbert B. Tanowitz, Murray Wittner

Research output: Contribution to journalArticle

86 Citations (Scopus)

Abstract

Toxoplasma gondii is a well-described ubiquitous Apicomplexan protozoan parasite that is an important opportunistic pathogen. The factors affecting the transition of tachyzoites to the latent bradyzoite stage remain to be defined. The induction of bradyzoite development in vitro has been linked to temperature, pH, mitochondrial inhibitors, sodium arsenite, and many of the other stressors associated with heat shock protein (hsp) induction. There is evidence for other organisms that hsps are developmentally regulated. Therefore, we examined whether hsp induction is an early event in bradyzoite differentiation. Extracellular and intracellular T. gondii cells, after exposure to pH 8.1 or 7.1, were analyzed for the expression of inducible hsp70 by using monoclonal antibody C92F3A-5 (specific to hsp70). Western blotting demonstrated that a 72-kDa protein reactive with C92F3A-5 (hsp70), which we believe is part of the hsp70 family, is induced during bradyzoite development. By immunofluorescence and immunoelectron microscopy, we were able to demonstrate that hsp70 staining colocalized to T. gondii expressing bradyzoite-specific antigens and the presence of hsp70 in bradyzoites isolated from mouse brain. Quercetin, a biofiavonoid which inhibits the synthesis of hsp90, hsp70, and hsp27, suppresses the induction of bradyzoite development in vitro. Reverse transcription-PCR with conserved hsp70 primers demonstrated an increase in hsp70 in T. gondii on exposure to conditions which induce bradyzoite formation. A T. gondii hsp70 was subsequently cloned and sequenced by using this amplified fragment. We believe our evidence suggests that hsps are important in the process of bradyzoite differentiation.

Original languageEnglish (US)
Pages (from-to)3295-3302
Number of pages8
JournalInfection and Immunity
Volume66
Issue number7
StatePublished - Jul 1998

Fingerprint

Toxoplasma
Heat-Shock Proteins
Immunoelectron Microscopy
Quercetin
Fluorescence Microscopy
Reverse Transcription
Parasites
Western Blotting
Monoclonal Antibodies
Staining and Labeling
Antigens
Polymerase Chain Reaction
Temperature
Brain
Proteins
In Vitro Techniques

ASJC Scopus subject areas

  • Immunology

Cite this

Weiss, L. M., Ma, Y. F., Takvorian, P. M., Tanowitz, H. B., & Wittner, M. (1998). Bradyzoite development in Toxoplasma gondii and the hsp70 stress response. Infection and Immunity, 66(7), 3295-3302.

Bradyzoite development in Toxoplasma gondii and the hsp70 stress response. / Weiss, Louis M.; Ma, Yan Fen; Takvorian, Peter M.; Tanowitz, Herbert B.; Wittner, Murray.

In: Infection and Immunity, Vol. 66, No. 7, 07.1998, p. 3295-3302.

Research output: Contribution to journalArticle

Weiss, LM, Ma, YF, Takvorian, PM, Tanowitz, HB & Wittner, M 1998, 'Bradyzoite development in Toxoplasma gondii and the hsp70 stress response', Infection and Immunity, vol. 66, no. 7, pp. 3295-3302.
Weiss, Louis M. ; Ma, Yan Fen ; Takvorian, Peter M. ; Tanowitz, Herbert B. ; Wittner, Murray. / Bradyzoite development in Toxoplasma gondii and the hsp70 stress response. In: Infection and Immunity. 1998 ; Vol. 66, No. 7. pp. 3295-3302.
@article{7537f45b895a4db0813f3f8ef3f26a0f,
title = "Bradyzoite development in Toxoplasma gondii and the hsp70 stress response",
abstract = "Toxoplasma gondii is a well-described ubiquitous Apicomplexan protozoan parasite that is an important opportunistic pathogen. The factors affecting the transition of tachyzoites to the latent bradyzoite stage remain to be defined. The induction of bradyzoite development in vitro has been linked to temperature, pH, mitochondrial inhibitors, sodium arsenite, and many of the other stressors associated with heat shock protein (hsp) induction. There is evidence for other organisms that hsps are developmentally regulated. Therefore, we examined whether hsp induction is an early event in bradyzoite differentiation. Extracellular and intracellular T. gondii cells, after exposure to pH 8.1 or 7.1, were analyzed for the expression of inducible hsp70 by using monoclonal antibody C92F3A-5 (specific to hsp70). Western blotting demonstrated that a 72-kDa protein reactive with C92F3A-5 (hsp70), which we believe is part of the hsp70 family, is induced during bradyzoite development. By immunofluorescence and immunoelectron microscopy, we were able to demonstrate that hsp70 staining colocalized to T. gondii expressing bradyzoite-specific antigens and the presence of hsp70 in bradyzoites isolated from mouse brain. Quercetin, a biofiavonoid which inhibits the synthesis of hsp90, hsp70, and hsp27, suppresses the induction of bradyzoite development in vitro. Reverse transcription-PCR with conserved hsp70 primers demonstrated an increase in hsp70 in T. gondii on exposure to conditions which induce bradyzoite formation. A T. gondii hsp70 was subsequently cloned and sequenced by using this amplified fragment. We believe our evidence suggests that hsps are important in the process of bradyzoite differentiation.",
author = "Weiss, {Louis M.} and Ma, {Yan Fen} and Takvorian, {Peter M.} and Tanowitz, {Herbert B.} and Murray Wittner",
year = "1998",
month = "7",
language = "English (US)",
volume = "66",
pages = "3295--3302",
journal = "Infection and Immunity",
issn = "0019-9567",
publisher = "American Society for Microbiology",
number = "7",

}

TY - JOUR

T1 - Bradyzoite development in Toxoplasma gondii and the hsp70 stress response

AU - Weiss, Louis M.

AU - Ma, Yan Fen

AU - Takvorian, Peter M.

AU - Tanowitz, Herbert B.

AU - Wittner, Murray

PY - 1998/7

Y1 - 1998/7

N2 - Toxoplasma gondii is a well-described ubiquitous Apicomplexan protozoan parasite that is an important opportunistic pathogen. The factors affecting the transition of tachyzoites to the latent bradyzoite stage remain to be defined. The induction of bradyzoite development in vitro has been linked to temperature, pH, mitochondrial inhibitors, sodium arsenite, and many of the other stressors associated with heat shock protein (hsp) induction. There is evidence for other organisms that hsps are developmentally regulated. Therefore, we examined whether hsp induction is an early event in bradyzoite differentiation. Extracellular and intracellular T. gondii cells, after exposure to pH 8.1 or 7.1, were analyzed for the expression of inducible hsp70 by using monoclonal antibody C92F3A-5 (specific to hsp70). Western blotting demonstrated that a 72-kDa protein reactive with C92F3A-5 (hsp70), which we believe is part of the hsp70 family, is induced during bradyzoite development. By immunofluorescence and immunoelectron microscopy, we were able to demonstrate that hsp70 staining colocalized to T. gondii expressing bradyzoite-specific antigens and the presence of hsp70 in bradyzoites isolated from mouse brain. Quercetin, a biofiavonoid which inhibits the synthesis of hsp90, hsp70, and hsp27, suppresses the induction of bradyzoite development in vitro. Reverse transcription-PCR with conserved hsp70 primers demonstrated an increase in hsp70 in T. gondii on exposure to conditions which induce bradyzoite formation. A T. gondii hsp70 was subsequently cloned and sequenced by using this amplified fragment. We believe our evidence suggests that hsps are important in the process of bradyzoite differentiation.

AB - Toxoplasma gondii is a well-described ubiquitous Apicomplexan protozoan parasite that is an important opportunistic pathogen. The factors affecting the transition of tachyzoites to the latent bradyzoite stage remain to be defined. The induction of bradyzoite development in vitro has been linked to temperature, pH, mitochondrial inhibitors, sodium arsenite, and many of the other stressors associated with heat shock protein (hsp) induction. There is evidence for other organisms that hsps are developmentally regulated. Therefore, we examined whether hsp induction is an early event in bradyzoite differentiation. Extracellular and intracellular T. gondii cells, after exposure to pH 8.1 or 7.1, were analyzed for the expression of inducible hsp70 by using monoclonal antibody C92F3A-5 (specific to hsp70). Western blotting demonstrated that a 72-kDa protein reactive with C92F3A-5 (hsp70), which we believe is part of the hsp70 family, is induced during bradyzoite development. By immunofluorescence and immunoelectron microscopy, we were able to demonstrate that hsp70 staining colocalized to T. gondii expressing bradyzoite-specific antigens and the presence of hsp70 in bradyzoites isolated from mouse brain. Quercetin, a biofiavonoid which inhibits the synthesis of hsp90, hsp70, and hsp27, suppresses the induction of bradyzoite development in vitro. Reverse transcription-PCR with conserved hsp70 primers demonstrated an increase in hsp70 in T. gondii on exposure to conditions which induce bradyzoite formation. A T. gondii hsp70 was subsequently cloned and sequenced by using this amplified fragment. We believe our evidence suggests that hsps are important in the process of bradyzoite differentiation.

UR - http://www.scopus.com/inward/record.url?scp=2642654218&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2642654218&partnerID=8YFLogxK

M3 - Article

VL - 66

SP - 3295

EP - 3302

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 7

ER -