Proteomic analysis of egg white heparin-binding proteins: towards the identification of natural antibacterial molecules

Guyot, Nicolas; Labas, Valérie; Harichaux, Grégoire; Chessé, Magali; Poirier, J. C.; Nys, Yves; Réhault-Godbert, Sophie

doi:10.1038/srep27974

Cited by 50 publications

(70 citation statements)

References 84 publications

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“…After loading the crude sample (pool of ten individuals, five males and five females), the beads were washed extensively with the washing buffer until the absorbance at 220 nm reached zero, as previously reported (27). Elution of bound proteins was achieved with 50 mM Tris-HCl, 2 M NaCl, pH 7.4, until the absorbance at 220 nm reached zero.…”

Section: Purification Of Heparin Binding Proteinsmentioning

confidence: 99%

“…All samples (raw, flow-through and eluted fractions) were analyzed by SDS-PAGE. Protein profiles of egg white at ED11 and ED16 were compared to previously published data for experimental validation (27,30). For antibacterial assays, at least three independent assays were performed on Listeria monocytogenes and Salmonella enterica…”

Section: Experimental Design and Statistical Rationalementioning

confidence: 99%

“…We confirmed their orthology relationship using Ensembl database. Although they do not share the same gene symbol, LOC107051274 and CAO79236.1 conditions (27). Because AF protein composition at ED11 is thoroughly modified from ED12 onwards, due to the presence of egg white proteins masking the intrinsic protein composition of AF, we explored the antibacterial potential of AF at both ED11 and ED16 ( Fig.…”

Section: Gene Ontology Analysis Of the Chicken Af Proteome -An Analysmentioning

confidence: 99%

“…7A and 7B). Assays were performed on both pools of total AF, but also on fractions enriched in antibacterial molecules obtained after heparin-affinity chromatography (HBP, heparin-binding proteins), as previously described (27). At ED11, results show only weak antibacterial activity against Gram-positive L.m.…”

Section: Gene Ontology Analysis Of the Chicken Af Proteome -An Analysmentioning

confidence: 99%

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The Unique Features of Proteins Depicting the Chicken Amniotic Fluid

Silva¹,

Dombre²,

Brionne³

et al. 2019

Molecular & Cellular Proteomics

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SUMMARYIn many amniotes, the amniotic fluid is depicted as a dynamic milieu that participates in the protection of the embryo (cushioning, hydration, and immunity). However, in birds, the protein profile of the amniotic fluid remains unexplored, even though its proteomic signature is predicted to differ compared to human's. In fact, unlike humans, chicken amniotic fluid does not collect excretory products and its protein composition strikingly changes at mid-development due to the massive inflow of egg white proteins, which are thereafter swallowed by the embryo to support its growth. Using GeLC-MS/MS and shotgun strategies, we identified 91 non-redundant proteins delineating the chicken amniotic fluid proteome at day 11 of development, before egg white transfer. These proteins were essentially associated with the metabolism of nutrients, immune response and developmental processes. Forty-eight proteins were common to both chicken and human amniotic fluids, including serum albumin, apolipoprotein A1 and alpha-fetoprotein. We further investigated the effective role of the chicken amniotic fluid in innate defense and revealed that it exhibits significant antibacterial activity at day 11 of development. This antibacterial potential is drastically enhanced after egg white transfer, presumably due to lysozyme, avian betadefensin 11, vitelline membrane outer layer protein 1, and beta-microseminoprotein-like as the most likely antibacterial candidates. Interestingly, several proteins recovered in the chicken amniotic fluid prior and after egg white transfer are uniquely found in birds (ovalbumin and related proteins X and Y, avian beta-defensin 11) or oviparous species (vitellogenins 1 and 2, riboflavinbinding protein). This study provides an integrative overview of the chicken amniotic fluid proteome and opens stimulating perspectives in deciphering the role of the avian egg-specific proteins in embryonic development, including innate immunity. These proteins may constitute Proteomic specificities of the chicken amniotic fluid 3 valuable biomarkers for poultry production to detect hazardous situations (stress, infection, etc.), that may negatively affect the development of the chicken embryo. Proteomic specificities of the chicken amniotic fluid4

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Section: Purification Of Heparin Binding Proteinsmentioning

confidence: 99%

Section: Experimental Design and Statistical Rationalementioning

confidence: 99%

Section: Gene Ontology Analysis Of the Chicken Af Proteome -An Analysmentioning

confidence: 99%

Section: Gene Ontology Analysis Of the Chicken Af Proteome -An Analysmentioning

confidence: 99%

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The Unique Features of Proteins Depicting the Chicken Amniotic Fluid

Silva¹,

Dombre²,

Brionne³

et al. 2019

Molecular & Cellular Proteomics

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“…[30][31][32] Human BMP-2, by contrast, is a disulfide-linked homodimeric heparin-binding protein. 33,34 Egg white lysozyme is a monomeric heparin-binding protein, 35,36 which is also present in human milk. Purified lysozyme could be obtained from commercial sources in relatively large quantity and low cost.…”

mentioning

confidence: 99%

Incorporation of heparin-binding proteins into preformed dextran sulfate-chitosan nanoparticles

Zaman¹,

Wang²,

Blau³

et al. 2016

IJN

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Three‐dimensional structures of avian beta‐microseminoproteins: insight from the chicken egg‐specific beta‐microseminoprotein 3 paralog

et al. 2021

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Beta-microseminoproteins (MSMBs) are small disulfide-rich proteins that are conserved among vertebrates. These proteins exhibit diverse biological activities and were mainly reported to play a role in male fertility, immunity, and embryogenesis. In this work, we focused on the chicken MSMB3 protein that was previously depicted as an egg antibacterial protein. We report that MSMB3 protein is exclusively expressed in the reproductive tissues of laying hens (in contrast to chicken MSMB1 and MSMB2 paralogs), to be incorporated in the egg white during the process of egg formation. We also showed that chicken MSMB3 possesses highly conserved orthologs in bird species, including Neognathae and Palaeognathae. Chicken MSMB3 was purified from egg white using heparin affinity chromatography and was analyzed by top-down and bottom-up proteomics. Several proteoforms could be characterized, and a homodimer was further evidenced by NMR spectroscopy. The X-ray structure of chicken MSMB3 was solved for the first time, revealing that this protein adopts a novel dimeric arrangement. The highly cationic MSMB3 protein exhibits a distinct electrostatic distribution compared with chicken MSMB1 and MSMB2 structural models, and with published mammalian MSMB structures. The specific incorporation of MSMB3 paralog in the egg, and its phylogenetic conservation in birds together with its peculiar homodimer arrangement and physicochemical properties, suggests that the MSMB3 protein has evolved to play a critical role during the embryonic development of avian species. These new data are likely to stimulate research to elucidate the structure/function relationships of MSMB paralogs and orthologs in the animal kingdom.Beta-microseminoproteins (MSMBs) are nonglycosylated disulfide-rich miniproteins (molecular mass about 10 kDa) that have been identified in many animal species [1,2]. MSMB genes have been reported to exhibit strong conservation among vertebrates, although they share a relatively low level of sequence identity Abbreviations MALDI-TOF, matrix-assisted laser desorption ionization-time of flight; MSMB, microseminoprotein; nanoLC-MS/MS, nanoflow liquid chromatography-tandem mass spectrometry; PDB, protein data bank; PSP94, prostate secretory protein 94; SSP-2, small serum protein 2; TOCSY, total correlation spectroscopy.

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Proteomic analysis of egg white heparin-binding proteins: towards the identification of natural antibacterial molecules

Cited by 50 publications

References 84 publications

The Unique Features of Proteins Depicting the Chicken Amniotic Fluid

The Unique Features of Proteins Depicting the Chicken Amniotic Fluid

Incorporation of heparin-binding proteins into preformed dextran sulfate-chitosan nanoparticles

Three‐dimensional structures of avian beta‐microseminoproteins: insight from the chicken egg‐specific beta‐microseminoprotein 3 paralog

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