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

. 2020 Mar 13;11:418. doi: 10.3389/fmicb.2020.00418

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

Copyright © 2020 Forde, Kollanandi Ratheesh, Harvey, Thomson, Williamson, Biek and Opriessnig.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Schematic representation of the SpaA protein sequence. Based on To and Nagai, 2007. Numbers below indicate amino acid (AA) positions. Numbers within the blue boxes represent the typical number of repeat units. The signal sequence (AA 1-29) is thought to be associated with the secretion mechanism for this protein. The immunoprotective domain (AA 30-413) is the component conferring immunogenicity, and upon which typing schemes for SpaA have been developed. The role of the proline-rich region (415–447) has not been well described. Seven to 13 repeats of a 20-AA sequence containing a GW module make up the C-terminal domain of SpaA; these have a role in binding the SpaA protein to the bacterial cell surface.