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. 2015 Apr 18;16(1):321. doi: 10.1186/s12864-015-1509-1

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© Xiong et al. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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The PG recognition proteins of H. armigera. (A) Schematic representations of the H. armigera PGRP domain structures. Lengths of the amino acid sequences are indicated. (B) Phylogenetic analysis of PGRPs. The amino acid sequences of 9 H. armigera (Ha), 7 T. castaneum (Tc), 13 D. melanogastor (Dm), 11 B. mori (Bm), and 4 A. mellifera (Am) PGRPs are compared. Scale bar, 0.1 substitutions per site. The tree shows that HaPGRP and BmPGRPs form good orthologous groups, except for HaPGRP-LD. Red dots at nodes indicate bootstrap values greater than 800 from 1,000 trials. The putative 1:1 or 1:1:1 orthologs were connected by green lines. HaPGRP-LA, −LB, −LC, and -LD contain a transmembrane domain, while HaPGRP-SA1, −SA2, −SB1, −SB2, and -SD have a signal peptide. HaPGRP-SB1,-SB2, and -SD contain the key residues of the amidase activity that hydrolyzes PGs.