Protease-resistant single-domain antibodies inhibit Campylobacter jejuni motility

Download
  1. (PDF, 1 MB)
  2. Get@NRC: Protease-resistant single-domain antibodies inhibit Campylobacter jejuni motility (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1093/protein/gzu011
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleProtein Engineering, Design and Selection
ISSN1741-0134
Volume27
Issue6
Pages191198; # of pages: 8
SubjectC. jejuni; motility; protease resistance; protein stability; VHH
AbstractCamelid heavy-chain antibody variable domains (VHHs) are emerging as potential antimicrobial reagents. We have engineered a previously isolated VHH (FlagV1M), which binds Campylobacter jejuni flagella, for greater thermal and proteolytic stability. Mutants of FlagV1M were obtained from an error-prone polymerase chain reaction library that was panned in the presence of gastrointestinal (GI) proteases. Additional FlagV1M mutants were obtained through disulfide-bond engineering. Each approach produced V HHs with enhanced thermal stability and protease resistance. When the beneficial mutations from both approaches were combined, a hyperstabilized VHH was created with superior stability. The hyperstabilized V HH bound C. jejuni flagella with wild-type affinity and was capable of potently inhibiting C. jejuni motility in assays performed after sequential digestion with three major GI proteases, demonstrating the remarkable stability imparted to the VHH by combining our engineering approaches.
Publication date
PublisherOxford University Press
LanguageEnglish
AffiliationHuman Health Therapeutics; National Research Council Canada
Peer reviewedYes
NRC numberNRC-HHT-53217
NPARC number21272210
Export citationExport as RIS
Report a correctionReport a correction
Record identifier8c8f81ab-1aab-424c-8d30-13add7ed0b72
Record created2014-07-23
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)