# T CELL RESPONSES TO NON-H-2 ANTIGENS OF CHROMOSOME 17

> **NIH NIH R01** · BAYLOR COLLEGE OF MEDICINE · 1992 · $263,760

## Abstract

DESCRIPTION (Adapted from applicants abstract):  This application requests
renewal of support for the investigators studies of the "non-classical"
genes and gene products of the distal mouse major histocompatibility
complex.  Reflecting particularly important recent advances in their
investigation of the maternally transmitted antigen (Mta), the proposal
focuses specifically on work in that system.  Mta is the cell surface
product of three genes:  the first, Hmt, is encoded on the 17th chromosome
telomeric of TL and is thought to encode a class I heavy chain; the second,
in keeping with the general structure of class I antigens, is
beta2-microglobulin; the third, accounting for the maternally transmitted
polymorphism of the cell surface antigen, is a mitochondrial gene that
encodes a peptide, Mtf, corresponding to the N-terminus of the ND1 subunit
of the mitochondrial respiratory enzyme NADH dehydrogenase.  Mta is defined
on the basis of target cell lysis by cytolytic T lymphocytes (CTL).  The
investigators' recent studies strongly suggest that the selectivity of the
Mtf peptides for Hmt is a consequence of a specific binding pocket on Hmt
for the N-formyl moiety characteristic of proteins translated on
mitochondrial ribosomes (as well as proteins of prokaryotic origin).  These
workers hypothesize that the striking biochemical specificity of this class
I molecule reflects its physiological functions.  They will address five
specific issues:  1) using synthetic N-formyl-peptides and appropriate
analogs, they will define biochemical rules for Hmt-formyl-peptide
interactions; 2) they will continue efforts to isolate and characterize the
Hmt gene employing the strategy of retrovirus-mediated insertional
mutagenesis; 3) they will develop a cell-free system and exploit a class
I-inducible mutant cell line to assess physical and biochemical properties
of the Hmt-formyl peptide complex independently of CTL-mediated cell lysis;
4) by subcellular fractionation and pulse-chase analysis, Dr. Rich and
coworkers will investigate trafficking of Mtf peptides and cellular
assembly of the Mta complex; and 5) they will examine the biological
function(s) of Hmt, including the possibilities that it provides an
intracellular mechanism for binding, transport and disposal of potential
toxic formyl peptides and/or functions as an antigen-presenting molecule
specialized for presentation of antigens of bacterial origin.  These
workers believe it likely that the proposed studies of the structure and
specialized functions of Hmt will break new ground in the least understood
region of the MHC and will provide fundamental knowledge of general
importance in immunology and cell biology.

## Key facts

- **NIH application ID:** 3128288
- **Project number:** 5R01AI018882-10
- **Recipient organization:** BAYLOR COLLEGE OF MEDICINE
- **SAM.gov UEI:** FXKMA43NTV21
- **Principal Investigator:** ROBERT R. RICH
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1992
- **Award amount:** $263,760
- **Award type:** 5
- **Project period:** 1983-04-01 → 1996-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3128288

## Citation

> US National Institutes of Health, RePORTER application 3128288, T CELL RESPONSES TO NON-H-2 ANTIGENS OF CHROMOSOME 17 (5R01AI018882-10). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3128288. Licensed CC0.

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