Prothrombin Changes and Suggested Correlation With the Titers of Anti-SARS-CoV-2 IgGantibodies in Recently Recovered From SARS-CoV-2 Infection Healthy Volunteers

Document Type

Article

Publication Date

3-2024

Publication Title

Minerva Biotechnology and Biomolecular Research

Abstract

BACKGROUND: The coagulation system is critical in controlling hemorrhage. Scientific research has proven that SARS-CoV-2 infection leads to the destabilization of the coagulation process. However, very little is known about coagulopathy in the post-SARS-CoV-2 period. This study aimed to investigate prothrombin changes in relationship with anti-SARS-CoV-2 immunoglobulin G (IgG) antibodies titers in donors who recovered from the infection.
METHODS: Blood was collected from healthy volunteers, aged 25 to 45, who had recovered from COVID-19 3-6 months ago. All donors were allocated into groups based on anti-SARS-CoV-2 IgG antibodies titer levels: 0 (N.=20), 10±3 (N.=20), 55±5 (N.=20), 65±5 (N.=20), 75±5 (N.=20), 85±5 (N.=20), 95±5 (N.=20), 125±5 (N.=20), and 175±5 (N.=20) Index (S/C). This paper describes the most significant changes in prothrombin parameters among donor groups, depending on the titers of anti-SARS-CoV-2 IgG antibodies.
RESULTS: Prothrombin abnormalities may result in the pathologic conversion of fibrinogen to fibrin. We established the differences in various prothrombin parameters in donor groups with titers of anti-SARS-CoV-2 IgG antibodies ≥10±3 Index (S/C) and compared them to a reference point (donor groups with titer of anti-SARS-CoV-2 IgG antibodies 0 Index [S/C]).
CONCLUSIONS: The research demonstrated significant differences in the compounds and functions of prothrombin-origin molecules at all stages of their actions in the hemostasis system. The observed differences in the composition of these molecules indicate a potential change in the functioning of the hemostatic cascade, which can lead to the emergence of pathological conditions in the body.

Volume

36

Issue

1

First Page

13

Last Page

20

DOI

10.23736/S2724-542X.24.03051-7

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