{'fraction_non_alphanumeric': 0.02762854950115119, 'fraction_numerical': 0.039140445126630855, 'mean_word_length': 4.6943231441048034, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Mutational Evidence of Internal Fusion Loops in Herpes Simplex Virus Glycoprotein B

Volume 81, no. 9, p. 4858–4865, 2007. We reported our results characterizing several mutants derived from herpes simplex virus glycoprotein B. Each had been constructed using QuikChange (Stratagene) and cloned into a mammalian expression vector. In each case, we sequenced the mutated gB gene. We subsequently discovered that we had erred in analyzing our original sequencing data for two of the mutants, originally called Y179K and F262D. In fact the change at amino acid 179 was to a serine, so this mutant is now termed Y179S. The mutant originally called F262D turned out to be have the sequence of wild-type gB. Because of these errors, we remade Y179K and F262D and characterized them in all in the assays described in the original paper. The two mutants, Y179K and Y179S, have indistinguishable phenotypes in all assays, so that the original data reported in the paper are correct except for the designations of the mutations. In the case of F262D, we remade the correct mutant and found that its phenotype is inconclusive because it is poorly expressed on the cell surface ( (cid:2) 30% of wild type), possibly due to misfolding. Thus, all conclusions about F262D in the paper must be disregarded as incorrect.