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A label-free shotgun proteomics analysis of macadamia nut

ABSTRACT: In this study, we present a first proteomic overview of macadamia nut using a label-free shotgun proteomic approach and prediction of their proteins with potential allergenic activity and cross-reactivity via an in silico analysis. The defense response proteins were the most abundant group of proteins and accounted for 24% of the total abundance. The vicilin-like macadamia antimicrobial peptides 2-3 (MiAMP2) was the most abundant protein. The cascading of amino acid and carbohydrate metabolic pathways in macadamia nut were constructed and proposed for the first time. The in silico analysis revealed seed storage proteins (conglutins and vicilins), rubber elongation factor proteins, phosphate binding proteins, and detoxifying methylglyoxalases among others as proteins with allergenic and cross-reactive potential. The label-free shotgun proteomics study revealed valuable insight into the genetic and biological makeup of macadamia nut and potential proteins with predictive allergenic activity and cross-reactivity. Integration of genomics with the proteomic data will be indispensable for future molecular characterization of macadamia including allergens.

INSTRUMENT(S): LTQ FT

ORGANISM(S): Macadamia

TISSUE(S): Plant Cell, Cotyledon

DISEASE(S): Disease Free

SUBMITTER: sridevi muralidharan

LAB HEAD: N Alice Lee

PROVIDER: PXD015364 | Pride | 2020-01-13

REPOSITORIES: Pride

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Project description:Epitope mapping studies aim to identify the binding sites of antibody-antigen interactions to enhance the development of vaccines, diagnostics and immunotherapeutic compounds. However, mapping is a laborious process employing time- and resource-consuming M-bM-^@M-^Xwet benchM-bM-^@M-^Y techniques or epitope prediction software that are still in their infancy. For polymorphic antigens, another challenge is characterizing cross-reactivity between epitopes, teasing out distinctions between broadly cross-reactive responses, limited cross-reactions among variants and the truly type-specific responses. A refined understanding of cross-reactive antibody binding could guide the selection of the most informative subsets of variants for diagnostics and multivalent subunit vaccines. We explored the antibody binding reactivity of sera from human patients and Peromyscus leucopus rodents infected with Borrelia burgdorferi to the polymorphic outer surface protein C (OspC), an attractive candidate antigen for vaccine and improved diagnostics for Lyme disease. We constructed a protein microarray displaying 23 natural variants of OspC and quantified the degree of cross-reactive antibody binding between all pairs of variants, using Pearson correlation calculated on the reactivity values using three independent transforms of the raw data: (1) logarithmic, (2) rank, and (3) binary indicators. We observed that the global amino acid sequence identity between OspC pairs was a poor predictor of cross-reactive antibody binding. Then we asked if specific regions of the protein would better explain the observed cross-reactive binding and performed in silico screening of the linear sequence and 3-dimensional structure of OspC. This analysis pointed to the C-terminal helix of the structure as a major determinant of type-specific cross-reactive antibody binding. We developed bioinformatics methods to systematically analyze the relationship between local sequence/structure variation and cross-reactive antibody binding patterns among variants of a polymorphic antigen, and this method can be applied to other polymorphic antigens for which immune response data is available for multiple variants. Antibody profiling was performed on sera from Borrelia burgdorferi infected and non-infected humans and Peromyscus leucopus rodents against 23 variants of the surface protein OspC . For infected human serum samples, the OspC type of the infecting B. burgdorferi strain is unknown; for experimentally-infected P. leucopus serum samples, it is known. Of human serum samples, 55 were from infected individuals and 25 from naive controls. Of P. leucopus serum samples, 23 were from infected individuals and 7 were from naive controls.

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	F117686.xml	Xml
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	SriMacaShotgunScaffoldreanalysis161216lessthan1pcFDR.sf3	Other
	sri281014_01_5.RAW	Raw

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A label-free shotgun proteomics analysis of macadamia nut

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