# PROTEIN IN MINK ENCEPHALOPATHY

> **NIH NIH R01** · UNIVERSITY OF WISCONSIN-MADISON · 1992 · $93,421

## Abstract

The long term objectives of this application are to determine how to prion
protein becomes modified in infected animals, and how this modification
may produce cell injury.

Investigation of a new incident of transmissible mink encephalopathy (TME)
has resulted in the identification of two distinct disease syndromes in
hamsters.  The first has an incubation period of sixty-five days and has
the predominant clinical signs of hyperesthesia and cerebellar ataxia.  The
second syndrome has an incubation period of 160 days and is clinically
characterized by lethargy with no hyperesthesia or cerebellar ataxia.  Each
syndrome has been "cloned" by serial passage at high dilution.

Examination of the prion protein (PrP) in each of these syndromes has
revealed differences in solubilities, protease sensitivities, and molecular
weights.  This is the first time that PrP differences have been seen in two
distinct syndromes in a single outbred species.  Therefore, the differences
in PrP observed can not be due to changes in primary amino acid sequence,
but rather to posttranslational modification.

The specific aims of this proposal are to biochemically characterize the
PrPs from the two syndromes in an attempt to identify conformational and/or
other posttranslational modifications to these proteins which may effect
their processing within the cell and influence the disease syndrome
produced.  Furthermore, it may be possible to determine if the different
PrPs induce their associated syndromes in a "strain-specific" manner by
testing other infected species (mink, cattle, squirrel monkeys) for
specific PrP isoforms.

This proposal is relevant to human dementias of the Alzheimer's type
because it will attempt to determine biochemical differences in the
amyloid-like prion protein from two distinct clinical syndromes in
hamsters.  Changes identified may explain differences observed in the
solubility, protease sensitivity, and molecular weights of the proteins.
These findings may further relate to changes in protein processing in the
brain which influence the course and type of disease produced.

## Key facts

- **NIH application ID:** 3122593
- **Project number:** 5R01AG010669-02
- **Recipient organization:** UNIVERSITY OF WISCONSIN-MADISON
- **SAM.gov UEI:** LCLSJAGTNZQ7
- **Principal Investigator:** RICHARD FLOYD MARSH
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1992
- **Award amount:** $93,421
- **Award type:** 5
- **Project period:** 1991-09-29 → 1994-06-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3122593

## Citation

> US National Institutes of Health, RePORTER application 3122593, PROTEIN IN MINK ENCEPHALOPATHY (5R01AG010669-02). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3122593. Licensed CC0.

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