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Complement System01:27

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
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A complement C4-derived glycopeptide is a biomarker for PMM2-CDG.

Kishore Garapati1,2,3, Rohit Budhraja1, Mayank Saraswat1

  • 1Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota, USA.

JCI Insight
|April 8, 2024
PubMed
Summary

A novel glycopeptide biomarker, complement C4-derived Man5GlcNAc2, shows greater sensitivity than carbohydrate-deficient transferrin (CDT) testing for diagnosing PMM2-congenital disorder of glycosylation (CDG). This finding offers improved diagnostic accuracy for PMM2-CDG and other CDGs.

Keywords:
Genetic diseasesGeneticsGlycobiologyMetabolismProteomics

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Area of Science:

  • Biochemistry and Molecular Biology
  • Clinical Diagnostics
  • Glycomics

Background:

  • Diagnosis of PMM2-congenital disorder of glycosylation (PMM2-CDG), the most common CDG, typically relies on carbohydrate-deficient transferrin (CDT) and genetic testing.
  • Current diagnostic methods like CDT testing have limitations, including false negatives and normalization with age, necessitating more sensitive biomarkers.
  • Site-specific N-glycosylation alterations in sera of PMM2-CDG patients have not been previously reported.

Purpose of the Study:

  • To discover and validate novel glycopeptide alterations in sera of PMM2-CDG patients using advanced mass spectrometry.
  • To identify sensitive and specific biomarkers for PMM2-CDG diagnosis, potentially overcoming limitations of existing methods.
  • To explore the utility of identified biomarkers for therapeutic monitoring in PMM2-CDG and other CDGs.

Main Methods:

  • Multistep mass spectrometry-based N-glycoproteomics was employed to analyze sera from 72 individuals (patients and controls).
  • Comprehensive tandem mass tag (TMT)-based discovery experiments were performed, followed by method development for rapid profiling.
  • Targeted mass spectrometry was utilized for blinded validation in an independent sample set.

Main Results:

  • Analysis of 3,342 N-glycopeptides revealed decreased complex-type N-glycans and increased truncated, mannose-rich, and hybrid species in PMM2-CDG patients.
  • A novel glycopeptide from complement C4 (C4) carrying Man5GlcNAc2 was identified in 5 patients with normal CDT results, including those with mild disease or post-transplant.
  • This C4-derived Man5GlcNAc2 glycopeptide demonstrated greater sensitivity than CDT and was detected in individuals with variants of uncertain significance in PMM2.

Conclusions:

  • The complement C4-derived Man5GlcNAc2 glycopeptide is a promising biomarker for accurate diagnosis of PMM2-CDG.
  • This glycopeptide biomarker exhibits higher sensitivity compared to CDT testing, particularly in cases with normal CDT results or mild disease.
  • The identified biomarker holds potential for accurate diagnosis and therapeutic monitoring in patients with PMM2-CDG and potentially other congenital disorders of glycosylation.