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A Single Amino Acid Change In The Cytoplasmic Domain Allows The Influenza Virus Hemagglutinin To Be Endocytosed Through Coated Pits.

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A Single Amino Acid Change In The Cytoplasmic Domain Allows The Influenza Virus Hemagglutinin To Be Endocytosed Through Coated Pits.

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A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed

J Lazarovits¹, M Roth

¹University of Texas Southwestern Medical Center, Dallas 75235.

|June 3, 1988

View abstract on PubMed

Summary

This summary is machine-generated.

Introducing tyrosine at amino acid 543 of influenza hemagglutinin (HA) significantly enhances its endocytosis and recycling. This specific mutation is crucial for HA

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Area of Science:

Virology
Molecular Biology
Cell Biology

Background:

Influenza virus hemagglutinin (HA) is a key surface glycoprotein.
Understanding HA's endocytosis and recycling is vital for viral replication and host cell interaction.

Purpose of the Study:

To investigate the role of specific amino acids in the cytoplasmic domain of HA during endocytosis.
To identify mutations affecting HA internalization and recycling pathways.

Main Methods:

Site-specific mutagenesis was employed to alter amino acids in the HA cytoplasmic domain.
Mutant HA proteins were analyzed for changes in export rate, folding, antigenicity, and endocytosis.

Main Results:

Mutating three amino acids to tyrosine did not affect HA export, folding, or antigenicity.

Substitution of cysteine 543 with tyrosine dramatically increased HA internalization via coated pits and recycling.

Replacing cysteine 543 with phenylalanine or serine did not enhance HA internalization.

The mutant HA with tyrosine at position 543 showed no detectable phosphorylation.

Conclusions:

A specific tyrosine at position 543 in the HA cytoplasmic domain is essential for interaction with coated pits.
This tyrosine residue plays a critical role in mediating HA endocytosis and subsequent recycling.
The findings highlight a localized functional role for tyrosine in regulating protein trafficking.