Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia

Article


Deutscher, Ania T., Jenkins, Cheryl, Minion, F. Chris, Seymour, Lisa M., Padula, Matthew P., Dixon, Nicholas E., Walker, Mark J. and Djordjevic, Steven P.. 2010. "Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia." Molecular Microbiology. 78 (2), pp. 444-458. https://doi.org/10.1111/j.1365-2958.2010.07345.x
Article Title

Repeat regions R1 and R2 in the P97 paralogue Mhp271 of
Mycoplasma hyopneumoniae bind heparin, fibronectin and
porcine cilia

ERA Journal ID2501
Article CategoryArticle
AuthorsDeutscher, Ania T. (Author), Jenkins, Cheryl (Author), Minion, F. Chris (Author), Seymour, Lisa M. (Author), Padula, Matthew P. (Author), Dixon, Nicholas E. (Author), Walker, Mark J. (Author) and Djordjevic, Steven P. (Author)
Journal TitleMolecular Microbiology
Journal Citation78 (2), pp. 444-458
Number of Pages15
Year2010
Place of PublicationChichester, West Sussex. United Kingdom
ISSN0950-382X
1365-2958
Digital Object Identifier (DOI)https://doi.org/10.1111/j.1365-2958.2010.07345.x
Web Address (URL)http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2010.07345.x/pdf
Abstract

Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, adheres to ciliated respiratory epithelia resulting in ciliostasis and epithelial cell death. The cilium adhesin P97 (Mhp183) contains two repeat regions, designated R1 and R2, that play key roles in adherence. Eight pentapeptide repeats in R1 are sufficient to bind porcine cilia; however, both R1 and R2 are needed to bind heparin. Mhp271, a paralogue of P97, is the only other M. hyopneumoniae protein to contain both R1 and R2 repeats. These repeats are arranged as a set of three pentapeptide repeats (designated R1A271), two decapeptide repeats (designated R2271), and a second set of six pentapeptide repeats (designated R1B271). To determine their function, recombinant proteins containing R1A271 (F1271) and R2271-R1B271 (F2271) were constructed and used in in vitro binding assays. F2271, but not F1271, bound heparin (KD = 8.1 ± 0.4 nM), fibronectin (KD = 174 ± 13 nM) and porcine cilia. Pre-incubation of F2271 with 100 μM heparin blocked cilium binding by ~69%. Cell surface shaving with trypsin combined with two-dimensional liquid chromatography coupled to tandem mass spectrometry analysis identified Mhp271 as surface-exposed. Our data suggest that both R1 and R2 in Mhp271 are involved in binding to host molecules.

Keywordsadhesin; fibronectin; heparin; pentapeptide; recombinant protein; trypsin
ANZSRC Field of Research 2020300304. Animal protection (incl. pests and pathogens)
310910. Animal physiology - systems
300999. Veterinary sciences not elsewhere classified
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Byline AffiliationsUniversity of Wollongong
Elizabeth Macarthur Agricultural Institute, Australia
Iowa State University, United States
University of Technology Sydney
University of Queensland
Institution of OriginUniversity of Southern Queensland
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