VACV sA28 and sH2 in vitro protein binding analyses.

(A) Schematic representation of wild-type full-length H2 protein (aa 1–189) containing an N-terminal transmembrane domain (TM, aa 26–51). A Coomassie blue-stained SDS-PAGE gel of purified soluble sH2 (aa 91–189) is also shown. M: protein markers. (B) 2D...

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Bibliographic Details
Main Author:	Chi-Fei Kao (11414234) (author)
Other Authors:	Min-Hsin Tsai (17373720) (author), Kathleen Joyce Carillo (17373723) (author), Der-Lii Tzou (1897744) (author), Wen Chang (449265) (author)
Published:	2023
Subjects:	Biochemistry Medicine Microbiology Cell Biology Molecular Biology Biotechnology Immunology Cancer Infectious Diseases Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified mediate cell infection host cell entry different membrane layers two infectious forms mediated membrane fusion host membranes via div >< p determined residues important soluble h2 protein despite vaccinia virus vaccinia a28 protein h2 protein interaction membrane fusion h2 protein vaccinia virus h2 subcomplex h2 binding vitro </ upon binding unique system truncated version structurally assessed performed extensive multiple steps model full membrane components length a28 large number known homology functional analysis forms require date share also provide also expressed alanine mutagenesis a28 interacts
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VACV sA28 and sH2 <i>in vitro</i> protein binding analyses.

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