scispace - formally typeset
J

Jody L. Wilton

Researcher at University of Wollongong

Publications -  5
Citations -  347

Jody L. Wilton is an academic researcher from University of Wollongong. The author has contributed to research in topics: Mycoplasma hyopneumoniae & Porcine enzootic pneumonia. The author has an hindex of 5, co-authored 5 publications receiving 335 citations. Previous affiliations of Jody L. Wilton include New South Wales Department of Primary Industries.

Papers
More filters
Journal ArticleDOI

Proteolytic processing of the Mycoplasma hyopneumoniae cilium adhesin

TL;DR: It is shown that the cilium adhesin is proteolytically processed on the surface, with processing is complex, with cleavage occurring at different frequencies within multiple sites, and is strain specific.
Journal ArticleDOI

Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae

TL;DR: It is shown here that Mhp493 (P216), a paralogue of the cilium adhesin P97 (Mhp183), is cleaved between amino acids 1040 and 1089 generating surface‐accessible, heparin‐binding proteins P120 and P85, which are recognized by serum antibodies elicited during infection by M. hyopneumoniae.
Journal ArticleDOI

Reiterated repeat region variability in the ciliary adhesin gene of Mycoplasma hyopneumoniae

TL;DR: Variability in the number of amino acid repeats in RR1 amongst strains of M. hyopneumoniae may influence ciliary binding, and two putative integrin binding sites were identified in the 94 kDa ciliary adhesin.
Journal ArticleDOI

Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin

TL;DR: The ability of the cilium adhesin to bind heparin indicates that this molecule plays a multifunctional role in the adherence of M. hyopneumoniae to host respiratory surfaces and therefore has important implications with respect to the pathogenesis of this organism.
Journal ArticleDOI

The pyruvate dehydrogenase complex of Mycoplasma hyopneumoniae contains a novel lipoyl domain arrangement.

TL;DR: It is hypothesised that the lipoyl-binding domain of PdhD is performing the enzymatic function normally attributed to the PdhC lipoy lbinding domain in other organisms.