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IDENTIFICATION AND CHARACTERISATION OF TAXONOMICALLY INFORMATIVE PEPTIDES BY HIGH RESOLUTION MASS SPECTROMETRY FOR SOURCE IDENTIFICATION OF TRACE HAIR

ABSTRACT: In this study a proteomics workflow was developed for the discovery and characterization of taxonomically diagnostic hair peptides. Taxa were selected with a focus on relevance to crime scene investigation. A panel of 226 taxonomically informative peptides were identified and characterized, 209 which appear novel to this study. This included 59 peptides with single-species specificity, while the remainder were diagnostic due to restricted or convergent taxonomic distribution. The panel of taxa-discriminating markers was subsequently integrated into a forensic workflow. The developed workflow was used to analyze single fur-hair (20 mm), from four individuals from each species of interest. The data was processed using a curated protein database, providing an efficient and validated bioinformatics workflow that did not require prior source information. The method was able to classify all hairs analyzed with genus or species level resolution.

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat) Canis Lupus Vicugna Pacos Equus Caballus (horse) Homo Sapiens (human) Bos Taurus (bovine) Felis Catus (cat) (felis Silvestris Catus) Oryctolagus Cuniculus (rabbit) Sus Scrofa (pig) Camelus Dromedarius (dromedary) (arabian Camel) Cavia Porcellus (guinea Pig) Mus Musculus (mouse)

TISSUE(S): Hair

SUBMITTER: Romy Keane

LAB HEAD: Joel P A Gummer

PROVIDER: PXD065721 | Pride | 2026-05-13

REPOSITORIES: Pride

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			Action	DRS
	2023_07_24_010_Blank_13_6_REK.raw	Raw
	2023_07_24_014_Blank_19_6_REK.raw	Raw
	2023_07_24_037_H2O_Blank.raw	Raw
	240619_PVP0009A_CAT_250nLmin.raw	Raw
	240619_PVP0009B_CAT_250nLmin.raw	Raw

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Identification and Characterisation of Taxonomically Informative Peptides

Project description:Hair fibers serve as a prevalent and valuable form of biological trace evidence. Taxonomic classification of hair recovered during a criminal investigation provides crucial forensic intelligence and aids in evidence prioritisation. Traditional classification methods rely heavily on the analysis of hair shaft morphology, which requires individual analysis, can have limited taxonomic resolution, and is difficult to scale. Mass spectrometry-based proteomics can provide a biomolecular alternative by use of taxonomic amino acid polymorphisms to resolve the species of origin of trace evidence. In this study a proteomics workflow was developed for the discovery and characterization of taxonomically diagnostic hair peptides. Taxa were selected with a focus on relevance to crime scene investigation. A panel of 226 taxonomically informative peptides were identified and characterized, 209 of which are novel to this study. The biomarker panel includes 59 peptides with apparent single-species resolution, with remaining biomarkers being diagnostic in combination. The study also included 3 positive control keratin sequences where at least 2 are documented to occur in all mammals. The panel of taxa-discriminating markers was subsequently integrated into a forensic workflow, optimized for universal sample preparation and standardised LC/MS/MS data acquisition. The developed workflow was used to analyze single fur-hair shafts (20 mm), from four individuals from each species of interest. The data was further processed using a curated protein database, an efficient and validated bioinformatics workflow. The method was able to classify all hairs analysed with genus or species level resolution without prior source information.

2026-05-13 | PXD062555 | Pride

Profiling Protein Expression Levels and Genetically Variant Peptides in Human Hair From Different Body Sites

Project description:Proteins of the human hair shaft contain a wealth of information about the coding regions of the person’s genome from whom the hair is derived. Commonly found at crime scenes, hair shafts may thus provide useful forensic evidence if the information they contain can be exploited. Present experiments show that hair shafts from four different anatomic sites are similarly useful in distinguishing individuals by protein profiling. However, the results demonstrated that protein profiles were dependent on anatomic site, indicating that a proper comparison requires matching the sites of origin. The differences in profile offer the prospect of determining the site of origin of hair by comparison with profiles of shafts from other anatomic sites. By contrast, the genetically variant peptides detected in the protein digests, that map to non-synonymous single nucleotide polymorphisms in subject DNA, were detectable regardless of the anatomic origin of the hair shafts. The resulting profiles of genetically variant peptides were more dependent on a subject’s genotype than on the anatomic origin of the hair shaft. Individual identification therefore can be based on peptide profiles regardless of body location. This study demonstrates the utility of proteomic analysis for increasing the forensic value of hair shaft evidence.

2019-04-04 | PXD011732 | Pride

Optimal Processing for Proteomic Genotyping of Single Human Hairs

Project description:The human hair proteome offers new insight in the field of human identification. Hair often contains DNA that has been degraded due to the process of cornification. The smaller fragments of DNA present a challenge for obtaining useful information concerning the identity of the donor. Proteomic genotyping offers an alternative approach which starts with protein, a biomolecule abundant in the hair shaft. Nonsynonymous single nucleotide polymorphisms may be detected in the sequence of these proteins, allowing the inference of SNP genotypes. Population genetics-based information from these genotypes may be used to calculate random match probability or even infer ancestry. The current challenge of this research is to optimize processing chemistry in order to maximize genetic information from a single human hair shaft. Results indicate that optimal conditions for proteomic analysis of a single human hair include 6 hrs of reduction with 100 mM dithiothreitol at room temperature, alkylation with 200 mM iodoacetamide for 45 min, and 6 hrs of digestion with two 1:50 (enzyme:protein) additions of stabilized trypsin at room temperature, with stirring incorporated into all three steps. Our final conditions using optimized temperatures and incubation times for disulfide reduction and protein digestion produced random match probabilities of up to 1 in 624 million from a single hair with a median value of 1 in 1.1 million, compared to a maximum random match probability of 1 in 1380 and a median value of 1 in 24 for the original processing method.

2020-06-10 | PXD016155 | Pride

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Project description:With their stereotyped dimensions and orderly arrangement, as well as their essential role in auditory and vestibular function, stereocilia of sensory hair cells provide a particularly prominent example of the importance of cellular actin protrusions. Uniformity of actin packing in stereocilia is mediated by actin crosslinkers of the plastin, fascin, and espin families. While mice lacking ESPN (espin) have no vestibular function, we found that mice that either lacked PLS1 (plastin 1) or had nonfunctional FSCN2 (fascin 2) had vestibular function that was modestly reduced, with double-mutant mice being more strongly affected. Despite its outsized importance in functional assays, targeted mass spectrometry indicated that ESPN only accounted for ~15% of the total crosslinkers in mouse utricle stereocilia. PLS1 was the most abundant of the crosslinkers, and the second-most-abundant protein overall in stereocilia. Stereocilia lacking PLS1 were shorter and thinner than wild-type stereocilia. Surprisingly, while wild-type stereocilia had random liquid packing of their actin filaments, stereocilia lacking PLS1 had orderly hexagonal packing. Stereocilia with normal PLS1 but that lacked functional FSCN2 had normal liquid packing and normal dimensions. All three crosslinkers are required for normal stereocilia structure and function, but PLS1 biases stereocilia towards liquid packing, which allows stereocilia to grow to greater diameter.

2016-09-28 | PXD004044 | Pride

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Project description:The phospholipid- and Ca2+-binding protein annexin A5 (ANXA5) is the most abundant membrane-associated protein of ~P23 mouse vestibular hair bundles, present at ~15,000 copies per stereocilium, which is ~2% of the total protein there. Although seven other annexin genes are expressed in mouse utricles, mass spectrometry showed that none were upregulated in stereocilia of Anxa5-/- mice. Annexins have been proposed to mediate Ca2+-dependent repair of membrane lesions, which could be part of the repair mechanism in hair cells after noise damage. Nevertheless, Anxa5-/- mice not only have normal hearing or balance, but are identical to wild-type mice in their temporary or permanent hearing changes following noise exposure. We suggest that the significant amounts of ANXA2 and ANXA6 that are present in the hair-cell cytoplasm can substitute in any function carried out by ANXA5, and that ANXA5 may be playing a hitchhiker role in the bundle. These results demonstrate that abundance of a protein in a specific compartment or cellular structure does not necessarily imply functional significance.

2016-06-09 | PXD003005 | Pride

Palaeoproteomics identifies beaver fur and fur trade in Danish high-status Viking Age burials

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