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. Author manuscript; available in PMC: 2010 Oct 1.
Published in final edited form as: J Immunol. 2009 Sep 14;183(7):4628–4638. doi: 10.4049/jimmunol.0803300

Figure 1.

Figure 1

Schematic representation of P1 and regions contributing to epitope formation. (A) Schematic representation of the primary sequence of P1 and its relevant domains. (B) Segments of P1 or combinations thereof currently known to achieve epitopes recognized by a panel of eleven different anti-P1 MAbs. Anti-P1 MAbs that map to the C-terminus of P1 are not reactive with whole bacterial cells. MAb 3-8D reacts predominantly with breakdown products of P1 as well as with a sub-cloned A-region polypeptide. It is also poorly reactive with whole bacterial cells. (C) Schematic representation of recombinant P1 polypeptides NR21, CK1 and CK2. The in-frame deletion construct NR21 was initially generated during studies to evaluate the contribution of the P-region to P1 epitopes. (D) Reactivity of anti-P1 MAbs with CG14 (full-length recombinant P1) and polypeptide NR21 by Western Blot.