# ANAEROBIC ENERGY METABOLISM OF PARASITIC HELMINTHS

> **NIH NIH R01** · BOWLING GREEN STATE UNIVERSITY · 1992 · $105,376

## Abstract

The parasitic helminths continue to represent serious global concerns
that impact significantly both on human and veterinary medicine.
Considered within the framework of effective chemotherapy, these
pathogens present a unique problem.  It is now clear that in marked
contrast to corresponding viral, bacterial, mycotic and protozoan
disease-causing systems, the helminths present an unmatched level of
complexity because chemotherapeutic elimination of helminth infections is
generally not amenable to agents that would solely disrupt proliferation.
Indeed, where determined, a large number of agents that display
chemotherapeutic efficacy do so by disrupting energy-generating and
related sequences, neurotransmission or neuromuscular events.  Thus, in
the development of any multi-faceted approach to the effective
chemotherapy of the parasitic helminths, it is essential to understand
and evaluate the energetic mechanisms of these systems.  Such evaluations
are required in the determination of vulnerable sites for specific
chemotherapeutic attack and present a reasonable approach to the
development and assay of agents displaying chemotherapeutic efficacy.

A vast number of the helminth parasites are predominantly anaerobic and
accumulate succinate, or products derived from succinate, as the result
of carbohydrate dissimilation.  Succinate is formed by the required,
anaerobic, mitochondrial electron transport mechanism of the helminths.
The research proposed addresses a totally novel aspect of the
biochemistry of parasitic helminths, viz., the metabolic impact of proton
translocation/membrane energization as this relates to the
characteristically anaerobic, mitochondrial energetics of the helminths.
Data accumulated, employing the adult cestode, Hymenolepis diminuta as
the model, indicate that mitochondrial, inner membrane-associated
NADPH:NAD transhydrogenase engages not only in hydride transfer but in
transmembrane proton translocation.  Therefore, characterization of this
enzyme and the development of a proton-translocating, NADPH:NAD
transhydrogenase-containing liposome system are proposed.  The H.
diminuta electron transport mechanism also will be studied in terms of
characterization/isolation of NADH dehydrogenase, "Complex I"
(NADH-rhodoquinone reductase) and Mg++-dependent ATPase.  Furthermore, a
study of the possible occurrence of an NADPH:NAD system in the adult
nematode, Ascaris suum, will aid considerably in the elucidation of
functional significance.  Lastly, comparative studies of the A. suum
"Complex 1" and electron transport system, in light of the H. diminuta
model, will contribute significantly to an understanding of the molecular
make up of mitochondrial electron transport in the helminths.

## Key facts

- **NIH application ID:** 3126257
- **Project number:** 2R01AI015597-10A2
- **Recipient organization:** BOWLING GREEN STATE UNIVERSITY
- **SAM.gov UEI:** SLT3EB6G3FA9
- **Principal Investigator:** CARMEN F FIORAVANTI
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1992
- **Award amount:** $105,376
- **Award type:** 2
- **Project period:** 1979-01-01 → 1997-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126257

## Citation

> US National Institutes of Health, RePORTER application 3126257, ANAEROBIC ENERGY METABOLISM OF PARASITIC HELMINTHS (2R01AI015597-10A2). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126257. Licensed CC0.

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