# SIALYLOLIGOSACCHARIDE RECEPTORS OF ANIMAL VIRUSES

> **NIH NIH R01** · UNIVERSITY OF CALIFORNIA LOS ANGELES · 1987 · $228,248

## Abstract

The long term goal of the proposed research is to understand the
biology of the interactions of influenza viruses with host cell
receptors at the molecular level.  In past years, the applicant and
coworkers have investigated the specificity of influenza isolates
for their recognition of sialic acid containing carbohydrate
receptor determinants on cell surface glycoproteins and
glycolipids.  Of particular interest was that human isolates with
the H3 hemagglutinin specifically recognized sialosides with the
SAa2, 6Gal linkage while avian and equine isolates with the same
hemagglutinin gene bound the SAa2,3Gal linkage.  Laboratory
selection directed at differences in receptor specificity enabled
isolation of variants with the opposite receptor type from both
human and avian parent viruses.  In collaboration with John Skehel
and Don Wiley, the major differences in receptor specificity in
the variants and the field isolates was shown to be due to a single
amino acid at residue 226 which resides in the receptor binding
pocket of the hemagglutinin.  Insights have been gained into the
basis of selection of these viruses in nature.  The applicant's lab
has also participated in the elucidation of the unique receptor
determinant of influenza C virus as 9-0-acetyl-neuraminic acid.

In the next project period the detailed molecular interactions
between sialyloligosaccharide receptor determinants with and the
hemagglutinin binding pocket will continue to be investigated with
Don Wiley and John Skehel.  Artificial sialic acid analogs will be
screened to identify potent receptor site inhibitors.  The role of
the potent glycoprotein inhibitor, equine a2-macroglobulin, in
maintaining the receptor specificity of equine H3 isolates will be
studied.  Differential virulence of the human H3 influenza viruses
and receptor variants will be evaluated in ferrets and primary pig
trachea epithelial cells.  Artificial sialic acid receptor
determinants of influenza C virus will be identified, and the role
of the unique receptor specificity of influenza C in its host range
will be examined.

The proposed studies will contribute to a more complete
molecular description of a virus-receptor interaction than
currently available for any other animal virus.  Further insights
are expected to be gained in understanding host mechanisms of
selection of receptor variants.  The results will also have
potential bearing on the development of live vaccines and small
molecular weight inhibitors of influenza virus infection.

## Key facts

- **NIH application ID:** 3126578
- **Project number:** 2R01AI016165-09
- **Recipient organization:** UNIVERSITY OF CALIFORNIA LOS ANGELES
- **SAM.gov UEI:** RN64EPNH8JC6
- **Principal Investigator:** JAMES C PAULSON
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $228,248
- **Award type:** 2
- **Project period:** 1979-08-01 → 1992-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126578

## Citation

> US National Institutes of Health, RePORTER application 3126578, SIALYLOLIGOSACCHARIDE RECEPTORS OF ANIMAL VIRUSES (2R01AI016165-09). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126578. Licensed CC0.

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