Immunoproteomics

Hess, Jennifer L.; Blazer, Levi L.; Romer, Terence; Faber, Lee E.; Buller, R. Mark; Boyle, Michael D. P.

doi:10.1016/j.jchromb.2004.07.047

Cited by 41 publications

(38 citation statements)

References 41 publications

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“…Other proteomic methodologies (e.g., shotgun, benzyldimethyl-n-hexadecylammonium chloride SDS-PAGE, agarose gel IEF) may provide data complementary to those presented here. Such approaches may have particular merit in resolving additional membrane, soluble matrix and high molecular weight proteins [68][69][70].…”

Section: Discussionmentioning

confidence: 99%

Immunoproteomic identification of bovine pericardium xenoantigens

et al. 2008

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Bovine pericardium is an important biomaterial with current application in glutaraldehyde-fixed bioprosthetic heart valves and possible future application as an unfixed biological scaffold for tissue engineering. The importance of both humoral and cell-mediated rejection responses toward fixed and unfixed xenogeneic tissues has become increasingly apparent. However, the full scope and specific identities of bovine pericardium proteins that can elicit an immune response remain largely unknown. In this study, an immunoproteomic approach was used to survey bovine pericardium proteins for their ability to elicit a humoral immune response in rabbits. A two-stage protein extraction protocol was used to separate bovine pericardium proteins into water-and lipid-soluble fractions. Two-dimensional gel electrophoresis was performed to separate the proteins from each fraction. Western blots were generated from two-dimensional gels of both bovine pericardium protein fractions. These blots were probed with serum from rabbits immunized with bovine pericardium and a secondary antibody was used to assess for IgG positivity. Western blots were compared to duplicate two-dimensional gels and proteins in matched spots were identified by tandem mass spectrometry. Thirty-one putative protein antigens were identified, eight of which are known to be antigenic from previous studies. All of the putative antigens demonstrated progressive staining intensity with increasing days of post-exposure serum. Identified antigenic proteins represented a variety of functional and structural protein types, and included both cellular and matrix proteins. The results of this study have implications for the use of bovine pericardium as a biomaterial in bioprostheses and tissue engineering applications, as well as xenotransplantation in general.

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Section: Discussionmentioning

confidence: 99%

Immunoproteomic identification of bovine pericardium xenoantigens

et al. 2008

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“…For diagnostic applications, antibodies have many appealing features, which make them attractive biomarkers [8,9]. First, the amplification cascade governed by the humoral immune system causes a surplus of circulating antibodies after appearance of the cognate (low abundance) antigen in the human body.…”

Section: Scope Of This Review: Immunoproteomics Towards Diagnostics Amentioning

confidence: 99%

Immunoproteomics: From biomarker discovery to diagnostic applications

Tjalsma

Schaeps

Swinkels

2008

Proteomics Clinical Apps

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Circulating antibodies reflect a molecular imprint of antigens that are related to autoimmune diseases, cancer or infection. Importantly, serum antibodies are useful clinical markers as they carry diagnostic information from all around the human body. Moreover, the amplification cascade governed by the humoral immune system causes a surplus of circulating antibodies after appearance of the corresponding (low abundance) antigen. In combination with the fact that antibodies are highly stable compared to many other serum proteins, they seem ideal to be implemented in clinical diagnostic assays for the detection of antigen-associated diseases. This review summarises advances in immunoproteomics with respect to technologies for biomarker discovery, with special emphasis on recently developed gel-free MS-based approaches, and looks forward to potential immunoproteomic applications in diagnostic medicine.

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“…In the present study, we employed such an approach, "immunoproteomics" [14][15][16], to identify the potential immunogens from five serovars of Leptospira reference strains that reacted to the sera from patients with leptospirosis. The data obtained from our study may lead to the development of new diagnostic tests and also to vaccine discovery.…”

Section: Introductionmentioning

confidence: 99%

Application of immunoproteomics to leptospirosis: towards clinical diagnostics and vaccine discovery

Kositanont

Saetun

Krittanai

et al. 2007

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Each of the currently available methods for serodiagnosis of leptospirosis, including the microscopic agglutination test (MAT), has its own drawback(s) when used in clinical practice. A new diagnostic test is therefore required for an earlier and more accurate diagnosis of leptospirosis. We applied immunoproteomics to define potential immunogens from five serovars of Leptospira reference strains. A leptospiral whole cell lysate from each serovar was used as the antigen to react with IgG and IgM in the sera from four patients with a positive MAT. Sera from four nonleptospirosis patients with a negative MAT were pooled and used as the negative control. 2-D Western blot analysis showed that the degree of immunoreactivity corresponded with the MAT titers. No immunoreactive spots were detected when the pooled control sera were used. A total of 24 protein spots immunoreacted with IgM and/or IgG from patients with leptospirosis. These immunoreactive proteins were identified by MALDI-TOF MS and were classified into five groups, including flagellar proteins, chaperones/heat shock proteins, transport proteins, metabolic enzymes, and hypothetical proteins. More immunoreactive spots were detected with antihuman IgG in the sera of all patients and with all the serovars of leptospires used. Some of the identified proteins immunoreacted only with IgG, whereas the others were detectable with both IgM and IgG. Among the immunoreactive proteins identified, FlaB proteins (flagellin and flagellar core protein) have been shown to have a potential role in clinical diagnostics and vaccine development. These data underscore the significant impact of immunoproteomics in clinical applications.

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Immunoproteomics

Cited by 41 publications

References 41 publications

Immunoproteomic identification of bovine pericardium xenoantigens

Immunoproteomic identification of bovine pericardium xenoantigens

Immunoproteomics: From biomarker discovery to diagnostic applications

Application of immunoproteomics to leptospirosis: towards clinical diagnostics and vaccine discovery

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