Localization of the membrane-associated region of vesicular stomatitis virus M protein at the N terminus, using the hydrophobic, photoreactive probe 125I-TID

Author:

Lenard J1,Vanderoef R1

Affiliation:

1. Department of Physiology and Biophysics, Robert Wood Johnson Medical School, University of Medicine and Dentistry, New Jersey, Piscataway 08854-5635.

Abstract

The membrane-reactive, photoactivatable probe 125I-TID [3-(trifluoromethyl)-3-(m-[125I]iodophenyl)-3H-diazirine] was found to label the M protein of vesicular stomatitis virus about 40% as much as G protein in intact virions, in agreement with labeling studies with other probes. By analyzing limited tryptic digestion and specific chemical cleavage products, the label was essentially entirely localized within the first 19, and probably within the first 5 to 10, amino acid residues at the N terminus, identifying this short amphipathic segment as the likely site of interaction of M protein with the viral bilayer.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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4. ntrodution f an cetylgroup t theN terinus.24:5422-5430.

5. Og den et al. (19) found that purified M protein bound to den et al. (19) found that purified M protein boundto5. Buerkler J. and J. Krebs. 1985. Structural studies of calmod

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