AUTHOR CORRECTION
Volume 79, no. 1, p. 79–86, 2005. Page 82, Fig. 2 and 3: Part of our 2005 report characterized the enzymatic activity of a soluble form of human hyaluronidase 2 (sHyal2) produced using a baculovirus protein expression system. We concluded that sHyal2 was a weak hyaluronidase that was active over a broad pH range. After publication, we determined that our purified sHyal2 was contaminated with a relatively small amount of a baculoviral protein (ODV-E66) that had hyaluronan lyase activity. We characterized a further purified sHyal2 as part of a later study (V. Vigdorovich, A. D. Miller, and R. K. Strong, J Virol 81:3124–3129, 2007, http://jvi.asm.org/content/81/7/3124.short), and we confirmed that sHyal2 is indeed a weak hyaluronidase but that it is active only over a restricted, acidic pH range. The baculoviral ODV-E66 protein has since been shown to be primarily a chondroitin lyase with lower hyaluronan lyase activity (N. Sugiura, Y. Setoyama, M. Chiba, K. Kimata, and H. Watanabe, J Biol Chem 286:29026–29034, 2011, http://dx.doi.org/10.1074/jbc.M111.251157).
Page 79, Abstract, lines 10 to 11; page 80, right column, lines 2 to 3; page 81, right column, 3rd paragraph; page 83, right column, lines 26 to 32: The statement that sHyal2 is active over a broad pH range is incorrect. As shown in our 2007 report, sHyal2 is active only over a restricted, acidic pH range. In addition, the detection of a contaminating hyaluronan lyase in our original sHyal2 preparations removed support for our claim that sHyal2 alone is able to digest hyaluronan past a 20-kDa intermediate. However, Fig. 3B, lane 5, of our 2007 report shows that further purified sHyal2 is indeed able to do so.
We provide this correction to alert readers of our earlier report to our later clarification.