Analysis Biomolecular Interactions of Vaccinia Virus (VACV) A27 Protein with Monoclonal Antibody by BLI (CAT#: STEM-MB-0124-CJ)

Introduction

Orthopoxviruses are a genus of DNA viruses of which four species are known to cause disease in humans: vaccinia virus (VACV), cowpox virus (CPXV), variola virus (VARV), and monkeypox virus (MPXV).
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VACV A27 is a 110 amino acid protein that consists of a signal peptide, an attachment domain or heparin binding site, a fusion domain, a coiled-coil domain. Structural studies indicate that in the monomer the N-terminal amino acids form a random and fairly flexible coil that is followed by a rigid α-helical region. The native protein exists as a hexamer and the α-helical region forms a coiled-coil in the self-assembling oligomerization region. Even though the heparin binding site (HBS) is found at the N-terminus, the oligomeric structure is required for heparin binding. The “KKPE” sequence within the HBS has been shown to be required for binding to heparin and this binding is sequence specific rather than a charge requirement.