Abstract

Chicken eggshell is a biomineral composed of 95% calcite calcium carbonate mineral and of 3.5% organic matrix proteins. The assembly of mineral and its structural organization is controlled by its organic matrix. In a recent study [1], we have used quantitative proteomic, bioinformatic and functional analyses to explore the distribution of 216 eggshell matrix proteins at four key stages of shell mineralization defined as: (1) widespread deposition of amorphous calcium carbonate (ACC), (2) ACC transformation into crystalline calcite aggregates, (3) formation of larger calcite crystal units and (4) rapid growth of calcite as columnar structure with preferential crystal orientation. The current article detailed the quantitative analysis performed at the four stages of shell mineralization to determine the proteins which are the most abundant. Additionally, we reported the enriched GO terms and described the presence of 35 antimicrobial proteins equally distributed at all stages to keep the egg free of bacteria and of 81 proteins, the function of which could not be ascribed.

Highlights

  • To cite this version: Pauline Marie, Valérie Labas, Aurélien Brionne, Grégoire Harichaux, Christelle Hennequet-Antier, et al

  • Data set for the proteomic inventory and quantitative analysis of chicken eggshell matrix proteins during the primary events of eggshell mineralization and the active growth phase of calcification

  • Label-free quantitative proteomic analyses based on spectral counting method, Scaffold 3 Q þ software was used to quantify the proteins at the four different stages of calcification

Read more

Summary

Collection of eggshell matrix samples and preparation for MS analyses

Eggs were collected on brown-laying hens at 5, 6, 7 and 16 h after previous oviposition as described in [1]. Protein identifications were accepted if they could be established at greater than 95.0% probability as specified by the Protein Prophet algorithm [6] and contained at least one sequenceunique peptide for global inventory and at least two sequence-unique peptides for quantitative analysis. The abundance of identified proteins was estimated by calculating the emPAI using Scaffold 4 Qþ software (version 4.2, Proteome Software, Portland, USA). Label-free quantitative proteomic analyses based on spectral counting method, Scaffold 3 Q þ software (version 3.4, Proteome Software, Portland, USA) was used to quantify the proteins at the four different stages of calcification. All proteins with greater than two sequence-unique peptides, identified in database with high confidence were considered for protein quantification. The mass spectrometry proteomic data have been deposited into the ProteomeXchange Consortium [2] via the PRIDE partner repository with the dataset identifier PXD001450

Data set analysis of avian eggshell matrix proteins
Findings
Quantitative dataset of avian eggshell matrix proteins
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call