Hypoxanthine-guanine phosphoribosyltransferase as a therapeutic target in protozoal infections

Buddy Ullman, D. Carter

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

The auxotrophy of parasitic protozoa for purines makes purine acquisition from the host a nutritional necessity for the survival and growth of these pathogens. The parasite hypoxanthine-guanine phosphoribosyltransferase (HGPRT) enzyme has been implicated as a critical enzyme in this purine salvage process. Moreover, the HGPRT enzyme in some parasites can also initiate the metabolism of purine base analogs that have little effect on the mammalian host. This implies that either inhibitors or substrates of HGPRT might serve as efficacious and selective agents for the treatment of parasitic diseases. This commentary provides an overview of recent molecular and biochemical studies on HGPRT proteins from parasitic protozoa and a discussion of the potential of HGPRT as a rational target for the chemotherapeutic manipulation of parasitic diseases.

Original languageEnglish (US)
Pages (from-to)29-40
Number of pages12
JournalInfectious Agents and Disease
Volume4
Issue number1
StatePublished - 1995

Fingerprint

Hypoxanthine Phosphoribosyltransferase
Infection
Parasitic Diseases
Parasites
Enzymes
Therapeutics
Purines
Growth
purine
Proteins

ASJC Scopus subject areas

  • Microbiology (medical)

Cite this

Hypoxanthine-guanine phosphoribosyltransferase as a therapeutic target in protozoal infections. / Ullman, Buddy; Carter, D.

In: Infectious Agents and Disease, Vol. 4, No. 1, 1995, p. 29-40.

Research output: Contribution to journalArticle

@article{5479ca6722f540e3a75160d57ab41dfd,
title = "Hypoxanthine-guanine phosphoribosyltransferase as a therapeutic target in protozoal infections",
abstract = "The auxotrophy of parasitic protozoa for purines makes purine acquisition from the host a nutritional necessity for the survival and growth of these pathogens. The parasite hypoxanthine-guanine phosphoribosyltransferase (HGPRT) enzyme has been implicated as a critical enzyme in this purine salvage process. Moreover, the HGPRT enzyme in some parasites can also initiate the metabolism of purine base analogs that have little effect on the mammalian host. This implies that either inhibitors or substrates of HGPRT might serve as efficacious and selective agents for the treatment of parasitic diseases. This commentary provides an overview of recent molecular and biochemical studies on HGPRT proteins from parasitic protozoa and a discussion of the potential of HGPRT as a rational target for the chemotherapeutic manipulation of parasitic diseases.",
author = "Buddy Ullman and D. Carter",
year = "1995",
language = "English (US)",
volume = "4",
pages = "29--40",
journal = "Infectious Agents and Disease",
issn = "1056-2044",
publisher = "Raven Press",
number = "1",

}

TY - JOUR

T1 - Hypoxanthine-guanine phosphoribosyltransferase as a therapeutic target in protozoal infections

AU - Ullman, Buddy

AU - Carter, D.

PY - 1995

Y1 - 1995

N2 - The auxotrophy of parasitic protozoa for purines makes purine acquisition from the host a nutritional necessity for the survival and growth of these pathogens. The parasite hypoxanthine-guanine phosphoribosyltransferase (HGPRT) enzyme has been implicated as a critical enzyme in this purine salvage process. Moreover, the HGPRT enzyme in some parasites can also initiate the metabolism of purine base analogs that have little effect on the mammalian host. This implies that either inhibitors or substrates of HGPRT might serve as efficacious and selective agents for the treatment of parasitic diseases. This commentary provides an overview of recent molecular and biochemical studies on HGPRT proteins from parasitic protozoa and a discussion of the potential of HGPRT as a rational target for the chemotherapeutic manipulation of parasitic diseases.

AB - The auxotrophy of parasitic protozoa for purines makes purine acquisition from the host a nutritional necessity for the survival and growth of these pathogens. The parasite hypoxanthine-guanine phosphoribosyltransferase (HGPRT) enzyme has been implicated as a critical enzyme in this purine salvage process. Moreover, the HGPRT enzyme in some parasites can also initiate the metabolism of purine base analogs that have little effect on the mammalian host. This implies that either inhibitors or substrates of HGPRT might serve as efficacious and selective agents for the treatment of parasitic diseases. This commentary provides an overview of recent molecular and biochemical studies on HGPRT proteins from parasitic protozoa and a discussion of the potential of HGPRT as a rational target for the chemotherapeutic manipulation of parasitic diseases.

UR - http://www.scopus.com/inward/record.url?scp=0028836011&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028836011&partnerID=8YFLogxK

M3 - Article

C2 - 7728354

AN - SCOPUS:0028836011

VL - 4

SP - 29

EP - 40

JO - Infectious Agents and Disease

JF - Infectious Agents and Disease

SN - 1056-2044

IS - 1

ER -