Proteomics

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Ancient palaeoimmunology: diving deeper with a two enzyme proteomics approach


ABSTRACT: This study investigates the efficacy of proteomic analysis of human remains to identify active Mycobacterium leprae infections in the past. Mycobacterial diseases, like leprosy, have plagued human populations for millennia. Thanks to effective treatment options, leprosy is not as widespread and deadly as in the past, yet remains endemic in certain regions with increasing concerns of strains becoming resistant to antibiotic treatments. We present a dual-enzyme, optimised extraction protocol, using trypsin and ProAlanase, to increase the recovery of non-collagenous proteins through a study of five individuals from a Mediaeval leprosarium cemetery, as well as four from a non-leprosy associated cemetery. Here we show that skeletal samples from the leprosarium individuals contain numerous immune proteins associated with modern leprosy, while those from a non-leprosy associated cemetery do not. Through this study, we advance a palaeoimmunology methodology and provide insights into the health of archaeological individuals and offer a means to triage samples for aDNA analysis.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Bone

SUBMITTER: Shevan Wilkin  

LAB HEAD: Dr. Shevan Wilkin

PROVIDER: PXD040419 | Pride | 2024-05-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20210315_002_S289326_ZH1114A1_rep.mgf Mgf
20210315_002_S289326_ZH1114A1_rep.mzML Mzml
20210315_002_S289326_ZH1114A1_rep.raw Raw
20210315_004_S289328_ZH1114A2.mgf Mgf
20210315_004_S289328_ZH1114A2.mzML Mzml
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This study investigates the efficacy of proteomic analysis of human remains to identify active infections in the past through the detection of pathogens and the host response to infection. We advance leprosy as a case study due to the sequestering of sufferers in leprosaria and the suggestive skeletal lesions that can result from the disease. Here we present a sequential enzyme extraction protocol, using trypsin followed by ProAlanase, to reduce the abundance of collagen peptides and in so doing  ...[more]

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