Profile and immunoreactivity of proteins from HPN tissue, and from Campylobacter jejuni (O:19) were investigated. Proteins were extracted, separated by SDS-PAGE, their cross reactivity monitored by Western blotting, and identified by nHPLC-nESI-HRMS analysis. Proteins from C. jejuni, at Mw ~70KDa were chaperone/co-chaperone proteins (GroEL, DnaK and HtpG). In the corresponding HPN band were serum albumin, neurofilament light peptide, cytoskeletal keratins and one HSP 70 and one HSP60. These chaperones reciprocally share high primary sequence homology and conservation of their known epitopes. These findings suggest that HSP chaperones may be suitable candidates involved in the molecular mimicry triggering GBS.
Guillain Barré syndrome (GBS) : new insights in the molecular mimicry between C. jejuni and human peripheral nerve (HPN) proteins / A. Loshaj-Shala, L. Regazzoni, A. Daci, M. Orioli, K. Brezovska, A.P. Panovska, G. Beretta, L. Suturkova. - In: JOURNAL OF NEUROIMMUNOLOGY. - ISSN 0165-5728. - 289(2015 Dec 15), pp. 168-176.
Guillain Barré syndrome (GBS) : new insights in the molecular mimicry between C. jejuni and human peripheral nerve (HPN) proteins
L. RegazzoniSecondo
;A. Daci;M. Orioli;G. BerettaPenultimo
;
2015
Abstract
Profile and immunoreactivity of proteins from HPN tissue, and from Campylobacter jejuni (O:19) were investigated. Proteins were extracted, separated by SDS-PAGE, their cross reactivity monitored by Western blotting, and identified by nHPLC-nESI-HRMS analysis. Proteins from C. jejuni, at Mw ~70KDa were chaperone/co-chaperone proteins (GroEL, DnaK and HtpG). In the corresponding HPN band were serum albumin, neurofilament light peptide, cytoskeletal keratins and one HSP 70 and one HSP60. These chaperones reciprocally share high primary sequence homology and conservation of their known epitopes. These findings suggest that HSP chaperones may be suitable candidates involved in the molecular mimicry triggering GBS.File | Dimensione | Formato | |
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