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. 2011 Jan 18;286(12):10097–10104. doi: 10.1074/jbc.M110.208140

FIGURE 1.

FIGURE 1.

Proteomic analyses of Mhp107. A, expression of Mhp107 occurs in vitro. ESI-MS/MS analysis of M. hyopneumoniae proteins extracted from an SDS-PAGE gel identified the amino acids shown in bold. Amino acids in italics and underlined italics indicate the predicted signal peptide sequence and transmembrane sequence, respectively. B, schematic representation of Mhp107, the putative 120-kDa protein encoded by mhp107. A predicted transmembrane and signal peptide sequence is depicted by the unfilled box. The position of the recombinant Mhp107 protein fragments (F1Mhp107-F3Mhp107) produced for this study are shown with amino acid positions indicated. The recombinant fragments include a 3.8-kDa polyhistidine region encoded by the expression vector. C, Coomassie-stained 12% SDS-PAGE gel of purified polyhistidine-tagged Mhp107 fragments. F1Mhp107 (lane 1), F2Mhp107 (lane 2), and F3Mhp107 (lane 3). D, immunoblot analyses using affinity-purified Mhp107 antisera. M. hyopneumoniae strain 232 whole cell lysates (lanes 1, 3, and 5) or aqueous phase (lanes 2, 4, and 6) were analyzed by immunoblot. Blots were probed with affinity-purified F1Mhp107 (lanes 1 and 2), F2Mhp107 (lanes 3 and 4), and F3Mhp107 (lanes 5 and 6) antisera.