Plasma Proteomics Unveil Novel Immune Signatures and Biomarkers upon SARS-CoV-2 Infection

Int J Mol Sci. 2023 Mar 27;24(7):6276. doi: 10.3390/ijms24076276.

Abstract

Several elements have an impact on COVID-19, including comorbidities, age and sex. To determine the protein profile changes in peripheral blood caused by a SARS-CoV-2 infection, a proximity extension assay was used to quantify 1387 proteins in plasma samples among 28 Finnish patients with COVID-19 with and without comorbidities and their controls. Key immune signatures, including CD4 and CD28, were changed in patients with comorbidities. Importantly, several unreported elevated proteins in patients with COVID-19, such as RBP2 and BST2, which show anti-microbial activity, along with proteins involved in extracellular matrix remodeling, including MATN2 and COL6A3, were identified. RNF41 was downregulated in patients compared to healthy controls. Our study demonstrates that SARS-CoV-2 infection causes distinct plasma protein changes in the presence of comorbidities despite the interpatient heterogeneity, and several novel potential biomarkers associated with a SARS-CoV-2 infection alone and in the presence of comorbidities were identified. Protein changes linked to the generation of SARS-CoV-2-specific antibodies, long-term effects and potential association with post-COVID-19 condition were revealed. Further study to characterize the identified plasma protein changes from larger cohorts with more diverse ethnicities of patients with COVID-19 combined with functional studies will facilitate the identification of novel diagnostic, prognostic biomarkers and potential therapeutic targets for patients with COVID-19.

Keywords: COVID-19; SARS-CoV-2; biomarker; immune signature; plasma proteomics.

MeSH terms

  • Antibodies, Viral
  • Biomarkers
  • Blood Proteins
  • COVID-19*
  • Humans
  • Proteomics
  • SARS-CoV-2
  • Ubiquitin-Protein Ligases

Substances

  • Antibodies, Viral
  • Blood Proteins
  • Biomarkers
  • RNF41 protein, human
  • Ubiquitin-Protein Ligases