The intriguing heterogeneity of human salivary proline-rich proteins

Manconi, Barbara; Castagnola, Massimo; Cabras, Tiziana; Olianas, Alessandra; Vitali, Alberto; Desiderio, Claudia; Sanna, Maria Teresa; Messana, Irene

doi:10.1016/j.jprot.2015.09.009

Cited by 52 publications

(47 citation statements)

References 94 publications

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“…Features of other IDPs can be incorporated into MAAB and used to identify IDPs in available genomes/transcriptomes. This would allow the identification of, for example, the repetitive domains of elastins (Roberts et al, 2015), salivary PRPs (Manconi et al, 2016), insect silks (Starrett et al, 2012), AGL proteins from arbuscular mycorrhizal fungi (Schultz and Harrison, 2008), and LATE EMBRYOGENESIS ABUNDANT proteins in plants (Sun et al, 2013), with low rates of false negatives and false positives.…”

Section: Versatility Of the Maab Pipeline For Hrgpsmentioning

confidence: 99%

Pipeline to Identify Hydroxyproline-Rich Glycoproteins

et al. 2017

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Intrinsically disordered proteins (IDPs) are functional proteins that lack a well-defined three-dimensional structure. The study of IDPs is a rapidly growing area as the crucial biological functions of more of these proteins are uncovered. In plants, IDPs are implicated in plant stress responses, signaling, and regulatory processes. A superfamily of cell wall proteins, the hydroxyprolinerich glycoproteins (HRGPs), have characteristic features of IDPs. Their protein backbones are rich in the disordering amino acid proline, they contain repeated sequence motifs and extensive posttranslational modifications (glycosylation), and they have been implicated in many biological functions. HRGPs are evolutionarily ancient, having been isolated from the protein-rich walls of chlorophyte algae to the cellulose-rich walls of embryophytes. Examination of HRGPs in a range of plant species should provide valuable insights into how they have evolved. Commonly divided into the arabinogalactan proteins, extensins, and proline-rich proteins, in reality, a continuum of structures exists within this diverse and heterogenous superfamily. An inability to accurately classify HRGPs leads to inconsistent gene ontologies limiting the identification of HRGP classes in existing and emerging omics data sets. We present a novel and robust motif and amino acid bias (MAAB) bioinformatics pipeline to classify HRGPs into 23 descriptive subclasses. Validation of MAAB was achieved using available genomic resources and then applied to the 1000 Plants transcriptome project (www.onekp.com) data set. Significant improvement in the detection of HRGPs using multiple-kmer transcriptome assembly methodology was observed. The MAAB pipeline is readily adaptable and can be modified to optimize the recovery of IDPs from other organisms.

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Section: Versatility Of the Maab Pipeline For Hrgpsmentioning

confidence: 99%

Pipeline to Identify Hydroxyproline-Rich Glycoproteins

et al. 2017

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“…APRPs belong to the highly unique family of proline-rich proteins -PRP, characterized by high proline content (25 to 42% of total amino acids), which affects protein conformation with a prominent preference of β-sheet structure [2,3]. Currently, a group of 10 distinct APRPs can be distinguished (APRP-1/2, APRP-3/4, parotid isoelectric-focusing slow/fast variant-PIF-s/f, parotid acidic protein -Pa, the double-band slow/fast isoform-Db-s/f and PC peptide), encoded by two genetic loci, PRH1 and PRH2 on chromosome 12 at p13.2 [4]. The PRH2 locus has two alleles and is responsible for the synthesis of principal isoforms of APRP-1/2 representing precursors of APRP-3/4 [3,5].…”

Section: Introductionmentioning

confidence: 99%

Human Salivary Acidic Proline-Rich Proteins (APRP-1/2) In Adult Patients With Dental Caries

Szkaradkiewicz-Karpiriska¹,

Sak²,

Goślińska-Kuźniarek³

et al. 2017

Dentistry

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Background: Acidic proline-rich proteins (APRPs) are manifested in human saliva in various phenotypes and represent its important component. The unique structure of their two isoforms. APRP-1/2 as well as their coupling to hydroxyapatite and formation of the acquired enamel pellicle are well known. Nevertheless, role of APRP-1/2 in adult patients with dental caries still remains unclear. The aim of this study was to analyze the levels of APRP-1/2 in saliva of adult patients with dental caries.

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“…In human saliva, many putative latent peptides derive from proline-rich proteins (PRPs). Within whole human saliva, PRPs account for more than 30% (w/w) of total protein content and for about 50-60% (w/w) of proteins secreted by parotid (Bennick 1982;Manconi et al 2016). From this group of proteins, three different families are distinguished, namely acidic PRPs (aPRPs), basic PRPs (bPRPs), and glycosylated (basic) PRPs (gPRPs) (Oppenheim et al 2007).…”

Section: Cryptides From Salivamentioning

confidence: 99%

Cryptides: latent peptides everywhere

Iavarone

Desiderio

Vitali

et al. 2018

Critical Reviews in Biochemistry and Molecular Biology

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Proteomic surveys with top-down platforms are today revealing thousands of naturally occurring fragments of bigger proteins. Some of them have not functional meaning because they derive from pathways responsible for protein degradation, but many have specific functions, often completely different from that one of the parent proteins. These peptides encrypted in the protein sequence are nowadays called cryptides. They are frequent in the animal and plant kingdoms and represent a new interesting -omic field of investigation. To point out how much widespread is their presence, we describe here the most studied cryptides from very common sources such as serum albumin, immunoglobulins, hemoglobin, and from saliva and milk proteins. Given its vastness, it is unfeasible to cover the topic exhaustively, therefore only several selected examples of cryptides from other sources are thereafter reported. Demanding is the development of new -omic platforms for the functional screening of new cryptides, which could provide suggestion for peptides and peptido-mimetics with variegate fields of application.

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The intriguing heterogeneity of human salivary proline-rich proteins

Cited by 52 publications

References 94 publications

Pipeline to Identify Hydroxyproline-Rich Glycoproteins

Pipeline to Identify Hydroxyproline-Rich Glycoproteins

Human Salivary Acidic Proline-Rich Proteins (APRP-1/2) In Adult Patients With Dental Caries

Cryptides: latent peptides everywhere

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