Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia
Article
Article Title | Repeat regions R1 and R2 in the P97 paralogue Mhp271 of |
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ERA Journal ID | 2501 |
Article Category | Article |
Authors | Deutscher, 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 Title | Molecular Microbiology |
Journal Citation | 78 (2), pp. 444-458 |
Number of Pages | 15 |
Year | 2010 |
Place of Publication | Chichester, West Sussex. United Kingdom |
ISSN | 0950-382X |
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. |
Keywords | adhesin; fibronectin; heparin; pentapeptide; recombinant protein; trypsin |
ANZSRC Field of Research 2020 | 300304. Animal protection (incl. pests and pathogens) |
310910. Animal physiology - systems | |
300999. Veterinary sciences not elsewhere classified | |
Public Notes | Files associated with this item cannot be displayed due to copyright restrictions. |
Byline Affiliations | University of Wollongong |
Elizabeth Macarthur Agricultural Institute, Australia | |
Iowa State University, United States | |
University of Technology Sydney | |
University of Queensland | |
Institution of Origin | University of Southern Queensland |
https://research.usq.edu.au/item/q25yx/repeat-regions-r1-and-r2-in-the-p97-paralogue-mhp271-of-mycoplasma-hyopneumoniae-bind-heparin-fibronectin-and-porcine-cilia
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