Abstract
Human bocavirus (HBoV) is a new parvovirus first discovered in 2005, which is associated with acute respiratory infection. Analysis of sequence homology has revealed that a putative phospholipase A 2 (PLA 2) motif exists in the VP1 unique region of HBoV. However, little is known about whether the VP1 unique region of HBoV has PLA 2 enzymatic activity and how these critical residues contribute to its PLA 2 activity. To address these issues, the VP1 unique region protein and four of its mutants, were expressed in Eschericha coli. The purified VP1 unique protein (VP1U) showed a typical Ca 2+-dependent secreted PLA 2-like (sPLA 2) activity, which was inhibited by sPLA 2-specific inhibitors in a time-dependent manner. Mutation of one of the amino acids (21Pro, 41His, 42Asp or 63Asp) in VP1U almost eliminated the sPLA 2 activity of HBoV VP1U. These data indicate that VP1U of HBoV has sPLA 2-like enzymatic activity, and these residues are crucial for its sPLA 2-like activity. Potentially, VP1U may be a target for the development of anti-viral drugs for HBoV.
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