Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2014 Oct 22;9(10):e110360. doi: 10.1371/journal.pone.0110360

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2014 May et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

PMC Copyright notice

(A) The putative hemagglutination motif (PHM; red) was predicted to adopt a hairpin structure of two anti-parallel β strands separated by a short disordered loop. (B) The motif (red, indicated by arrow) mapped to a low-complexity region near the carboxyterminal domain (CTD) of the M. synoviae adhesin protein VlhA cleavage product MSPA, shown here in the structure predicted for the Tunisian lineage of strain WVU1853^T. The N-terminal domain (NTD) of MSPA was predicted to have much greater 3-dimensional complexity. (C) The length of the disordered loop was predicted to be longer in PHM peptides that bound to avian erythrocyte membranes (representing Florida and Tunisian lineages of strain WVU1853^T and strains FMT, K5016 and K5395) than in the reduced-binding peptide mutant FMT-Ala9Gly and the non-binding peptide representing strain MS53.