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Article ; Online: Circulating Ficolin-2 and Ficolin-3 Form Heterocomplexes.

Jarlhelt, Ida / Pilely, Katrine / Clausen, Jytte Bryde / Skjoedt, Mikkel-Ole / Bayarri-Olmos, Rafael / Garred, Peter

Journal of immunology (Baltimore, Md. : 1950)

2020 Volume 204, Issue 7, Page(s) 1919–1928

Abstract: The complement system constitutes an important part of the innate immune system. The collectins and the ficolins are soluble pattern recognition molecules that contribute to complement activation via the lectin pathway. During previous experiments with ... ...

Abstract	The complement system constitutes an important part of the innate immune system. The collectins and the ficolins are soluble pattern recognition molecules that contribute to complement activation via the lectin pathway. During previous experiments with ficolin-2 and ficolin-3, we have observed that the molecules may interact. We therefore hypothesized the existence of stable ficolin-2/-3 heterocomplexes. We could demonstrate ficolin-2/-3 heterocomplexes in normal human serum and plasma by ELISA using Abs specific for ficolin-2 and ficolin-3. The formation of heteromeric protein complexes were validated by coimmunoprecipitation and Western blot analysis. When recombinant ficolin-2 and recombinant ficolin-3 were mixed, no complexes were formed. However, when coexpressing ficolin-2 and ficolin-3 in Chinese hamster ovary cells, we could detect ficolin-2/-3 heterocomplexes in the supernatant. Furthermore, we measured concentration of the ficolin-2/-3 heterocomplexes in arbitrary units in 94 healthy individuals. We also established the relationship between the concentrations of ficolin-2, ficolin-3, and the ficolin-2/-3 heterocomplexes. We observed that the concentration of the ficolin-2/-3 heterocomplex correlated significantly with ficolin-2 (ρ: 0.24,
MeSH term(s)	Animals ; CHO Cells ; Cell Line ; Collectins/metabolism ; Complement Activation/physiology ; Complement Pathway, Mannose-Binding Lectin/physiology ; Complement System Proteins/metabolism ; Cricetulus ; Humans ; Lectins/blood ; Mannose-Binding Protein-Associated Serine Proteases/metabolism ; Mice ; Ficolins
Chemical Substances	Collectins ; FCN3 protein, human ; Lectins ; Complement System Proteins (9007-36-7) ; Mannose-Binding Protein-Associated Serine Proteases (EC 3.4.21.-)
Language	English
Publishing date	2020-02-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1900694
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Article: The ficolin response to LPS challenge in mice

Jarlhelt, Ida / Garred, Peter / Genster, Ninette / Kirketerp-Møller, Nikolaj / Skjoedt, Mikkel-Ole

Molecular immunology. 2019 Apr., v. 108

2019

Abstract: The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we ... ...

Abstract	The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we investigated the ficolin A and ficolin B expression and protein distribution patterns in a mouse model of LPS-induced inflammation. The time- and tissue-specific expression of ficolin A and B was determined by real time PCR. Furthermore, ficolin protein levels in serum and bone marrow extracts from LPS challenged mice were determined by novel in-house developed sandwich ELISAs. Ficolin A was mainly expressed in liver and spleen. However, our data also suggested that ficolin A is expressed in bone marrow, which is the main site of ficolin B expression. The level of ficolin A and B expression was increased after stimulation with LPS in the investigated tissues. This was followed by a downregulation of expression, causing mRNA levels to return to baseline 24 h post LPS challenge. Protein levels appeared to follow the same pattern as the expression profiles, with an exception of ficolin B levels in serum, which kept increasing for 24 h. Ficolin A was likewise significantly increased in bronchoalveolar lavage fluid from mice infected with the fungi A. fumigatus, pointing towards a similar effect of the ficolins in non-sterile mouse models of inflammation. The results demonstrate that LPS-induced inflammation can induce a significant ficolin response, suggesting that the murine ficolins are acute phase reactants with increase in both mRNA expression and protein levels during systemic inflammation.
Keywords	acute phase proteins ; animal models ; blood serum ; bone marrow ; enzyme-linked immunosorbent assay ; fungi ; gene expression ; gene expression regulation ; inflammation ; lectins ; liver ; messenger RNA ; mice ; protein content ; quantitative polymerase chain reaction ; spleen
Language	English
Dates of publication	2019-04
Size	p. 121-127.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2019.02.013
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Article ; Online: The ficolin response to LPS challenge in mice.

Jarlhelt, Ida / Genster, Ninette / Kirketerp-Møller, Nikolaj / Skjoedt, Mikkel-Ole / Garred, Peter

Molecular immunology

2019 Volume 108, Page(s) 121–127

Abstract	The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we investigated the ficolin A and ficolin B expression and protein distribution patterns in a mouse model of LPS-induced inflammation. The time- and tissue-specific expression of ficolin A and B was determined by real time PCR. Furthermore, ficolin protein levels in serum and bone marrow extracts from LPS challenged mice were determined by novel in-house developed sandwich ELISAs. Ficolin A was mainly expressed in liver and spleen. However, our data also suggested that ficolin A is expressed in bone marrow, which is the main site of ficolin B expression. The level of ficolin A and B expression was increased after stimulation with LPS in the investigated tissues. This was followed by a downregulation of expression, causing mRNA levels to return to baseline 24 h post LPS challenge. Protein levels appeared to follow the same pattern as the expression profiles, with an exception of ficolin B levels in serum, which kept increasing for 24 h. Ficolin A was likewise significantly increased in bronchoalveolar lavage fluid from mice infected with the fungi A. fumigatus, pointing towards a similar effect of the ficolins in non-sterile mouse models of inflammation. The results demonstrate that LPS-induced inflammation can induce a significant ficolin response, suggesting that the murine ficolins are acute phase reactants with increase in both mRNA expression and protein levels during systemic inflammation.
MeSH term(s)	Animals ; Aspergillosis/immunology ; Aspergillosis/microbiology ; Aspergillus fumigatus/pathogenicity ; Biological Assay ; Bone Marrow/drug effects ; Bone Marrow/metabolism ; Bronchoalveolar Lavage Fluid ; Disease Models, Animal ; Lectins/blood ; Lectins/metabolism ; Lipopolysaccharides/pharmacology ; Mice ; Organ Specificity/drug effects ; Reproducibility of Results ; Ficolins
Chemical Substances	Lectins ; Lipopolysaccharides
Language	English
Publishing date	2019-02-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2019.02.013
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Article ; Online: Distinguishing SARS-CoV-2 infection and vaccine responses up to 18 months post-infection using nucleocapsid protein and receptor-binding domain antibodies.

Jarlhelt, Ida / Pérez-Alós, Laura / Bayarri-Olmos, Rafael / Hansen, Cecilie Bo / Petersen, Maria Skaalum / Weihe, Pál / Armenteros, Jose Juan Almagro / Madsen, Johannes Roth / Nielsen, Jacob Pohl Stangerup / Hilsted, Linda Maria / Iversen, Kasper Karmark / Bundgaard, Henning / Nielsen, Susanne Dam / Garred, Peter

Microbiology spectrum

2023 , Page(s) e0179623

Abstract: The prediction of the durability of immunity against COVID-19 is relevant, and longitudinal studies are essential for unraveling the details regarding protective SARS-CoV-2 antibody responses. It has become challenging to discriminate between COVID-19 ... ...

Abstract	The prediction of the durability of immunity against COVID-19 is relevant, and longitudinal studies are essential for unraveling the details regarding protective SARS-CoV-2 antibody responses. It has become challenging to discriminate between COVID-19 vaccine- and infection-induced immune responses since all approved vaccines in Europe and the USA are based on the viral spike (S) protein, which is also the most commonly used antigen in immunoassays measuring immunoglobulins (Igs) against SARS-CoV-2. We have developed a nucleocapsid (N) protein-based sandwich ELISA for detecting pan anti-SARS-CoV-2 Ig with a sensitivity and specificity of 97%. Generalized mixed models were used to determine the degree of long-term humoral immunity against the N protein and the receptor-binding domain (RBD) of the S protein in a cohort of infected individuals to distinguish between COVID-19 vaccine- and infection-induced immunity. N-specific waning could be observed in individuals who did not experience reinfection, while individuals who experienced reinfection had a new significant increase in N-specific Ig levels. In individuals that seroconverted without a reinfection, 70.1% remained anti-N seropositive after 550 days. The anti-RBD Ig dynamics were unaffected by reinfection but exhibited a clear increase in RBD-specific Ig when vaccination was initiated. In conclusion, a clear difference in the dynamics of the antibody response against N protein and RBD was observed over time. Anti-N protein-specific Igs can be detected up to 18 months after SARS-CoV-2 infection allowing long-term discrimination of infectious and vaccine antibody responses.IMPORTANCELongitudinal studies are essential to unravel details regarding the protective antibody responses after COVID-19 infection and vaccination. It has become challenging to distinguish long-term immune responses to SARS-CoV-2 infection and vaccination since most approved vaccines are based on the viral spike (S) protein, which is also mostly used in immunoassays measuring immunoglobulins (Igs) against SARS-CoV-2. We have developed a novel nucleocapsid (N) protein-based sandwich ELISA for detecting pan-anti-SARS-CoV-2 Ig, exhibiting high sensitivity and specificity. Generalized mixed models were used to determine long-term humoral immunity in a cohort of infected individuals from the Faroe Islands, distinguishing between COVID-19 vaccine- and infection-induced immunity. A clear difference in the dynamics of the antibody response against N protein and S protein was observed over time, and the anti-N protein-specific Igs could be detected up to 18 months after SARS-CoV-2 infection. This enables long-term discrimination between natural infection and vaccine-dependent antibody responses.
Language	English
Publishing date	2023-09-22
Publishing country	United States
Document type	Journal Article
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.01796-23
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Article ; Online: SARS-CoV-2 antibody dynamics over time and risk factors associated with infection and long COVID-19 symptoms in large working environments.

Hansen, Cecilie Bo / Dvoncova, Kristina / Pérez-Alós, Laura / Fogh, Kamille / Madsen, Johannes Roth / Garred, Caroline Hartwell / Jarlhelt, Ida / Nielsen, Pernille Brok / Petersen, Steffan Svejgaard / Fjordager, Charlotte Gandsø / Lauritsen, Klara Tølbøll / Hilsted, Linda / Boding, Lasse / Iversen, Kasper Karmark / Hyveled, Liselotte / Garred, Peter

Journal of internal medicine

2023 Volume 293, Issue 6, Page(s) 763–781

Abstract: Background: Factors influencing SARS-CoV-2 antibody dynamics, transmission, waning and long COVID-19 symptomatology are still not fully understood.: Methods: In the Danish section of the Novo Nordisk Group, we performed a prospective ... ...

Abstract	Background: Factors influencing SARS-CoV-2 antibody dynamics, transmission, waning and long COVID-19 symptomatology are still not fully understood. Methods: In the Danish section of the Novo Nordisk Group, we performed a prospective seroepidemiological study during the first and second waves of the COVID-19 pandemic. All employees and their household members (>18 years) were invited to participate in a baseline (June-August 2020), 6-month follow-up (December 2020-January 2021), and 12-month follow-up (August 2021) sampling. In total, 18,614 accepted and provided at least one blood sample and completed a questionnaire regarding socioeconomic background, health status, previous SARS-CoV-2 infection, and persistent symptoms. Total antibody and specific IgM, IgG and IgA levels against recombinant receptor binding domain were tested. Results: At baseline, the SARS-CoV-2-antibody seroprevalence was 3.9%. At 6-month follow-up, the seroprevalence was 9.1%, while at 12-month follow-up, the seroprevalence was 94.4% (after the vaccine roll-out). Male sex and younger age (18-40 years) were significant risk factors for seropositivity. From baseline to the 6-month sampling, we observed a substantial waning of IgM, IgG and IgA levels (p < 0.001), regardless of age, sex and initial antibody level. An increased antibody level was found in individuals infected prior to vaccination compared to vaccinated infection naïves (p < 0.0001). Approximately a third of the seropositive individuals reported one or more persistent COVID-19 symptoms, with anosmia and/or ageusia (17.5%) and fatigue (15.3%) being the most prevalent. Conclusion: The study provides a comprehensive insight into SARS-CoV-2 antibody seroprevalence following infection and vaccination, waning, persistent COVID-19 symptomatology and risk factors for seropositivity in large working environments.
MeSH term(s)	Humans ; Male ; Adolescent ; Young Adult ; Adult ; COVID-19/epidemiology ; Pandemics ; Post-Acute COVID-19 Syndrome ; Prospective Studies ; SARS-CoV-2 ; Seroepidemiologic Studies ; Working Conditions ; Antibodies, Viral ; Risk Factors ; Immunoglobulin A ; Immunoglobulin G ; Immunoglobulin M
Chemical Substances	Antibodies, Viral ; Immunoglobulin A ; Immunoglobulin G ; Immunoglobulin M
Language	English
Publishing date	2023-04-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	96274-0
ISSN	1365-2796 ; 0954-6820
ISSN (online)	1365-2796
ISSN	0954-6820
DOI	10.1111/joim.13637
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Article ; Online: Lectin Pathway Enzyme MASP-2 and Downstream Complement Activation in COVID-19.

Götz, Maximilian Peter / Skjoedt, Mikkel-Ole / Bayarri-Olmos, Rafael / Hansen, Cecilie Bo / Pérez-Alós, Laura / Jarlhelt, Ida / Benfield, Thomas / Rosbjerg, Anne / Garred, Peter

Journal of innate immunity

2022 Volume 15, Issue 1, Page(s) 122–135

Abstract: Mannose-binding lectin-associated serine protease 2 (MASP-2) is the main activator of the lectin complement pathway and has been suggested to be involved in the pathophysiology of coronavirus disease 2019 (COVID-19). To study a possible association ... ...

Abstract	Mannose-binding lectin-associated serine protease 2 (MASP-2) is the main activator of the lectin complement pathway and has been suggested to be involved in the pathophysiology of coronavirus disease 2019 (COVID-19). To study a possible association between MASP-2 and COVID-19, we aimed at developing a sensitive and reliable MASP-2 ELISA. From an array of novel mouse-monoclonal antibodies using recombinant MASP-2 as antigen, two clones were selected to create a sandwich ELISA. Plasma samples were obtained from 216 healthy controls, 347 convalescent COVID-19 patients, and 147 prospectively followed COVID-19 patients. The assay was specific towards MASP-2 and did not recognize the truncated MASP2 splice variant MAP-2 (MAp19). The limit of quantification was shown to be 0.1 ng/mL. MASP-2 concentration was found to be stable after multiple freeze-thaw cycles. In healthy controls, the mean MASP-2 concentration was 524 ng/mL (95% CI: 496.5-551.6). No significant difference was found in the MASP-2 concentrations between COVID-19 convalescent samples and controls. However, a significant increase was observed in prospectively followed COVID-19 patients (mean: 834 ng/mL [95% CI: 765.3-902.7, p < 0.0001]). In these patients, MASP-2 concentration correlated significantly with the concentrations of the terminal complement complex (ρ = 0.3596, p < 0.0001), with the lectin pathway pattern recognition molecules ficolin-2 (ρ = 0.2906, p = 0.0004) and ficolin-3 (ρ = 0.3952, p < 0.0001) and with C-reactive protein (ρ = 0.3292, p = 0.0002). Overall, we developed a specific quantitative MASP-2 sandwich ELISA. MASP-2 correlated with complement activation and inflammatory markers in COVID-19 patients, underscoring a possible role of MASP-2 in COVID-19 pathophysiology.
MeSH term(s)	Animals ; Humans ; Mice ; Complement Activation/physiology ; Complement Pathway, Mannose-Binding Lectin ; COVID-19 ; Ficolins ; Lectins ; Mannose-Binding Lectin/metabolism ; Mannose-Binding Protein-Associated Serine Proteases/analysis ; Mannose-Binding Protein-Associated Serine Proteases/metabolism
Chemical Substances	Ficolins ; Lectins ; Mannose-Binding Lectin ; Mannose-Binding Protein-Associated Serine Proteases (EC 3.4.21.-) ; MASP-2 protein, mouse (EC 3.4.21.-) ; MASP2 protein, human (EC 3.4.21.-)
Language	English
Publishing date	2022-07-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2454158-8
ISSN	1662-8128 ; 1662-811X
ISSN (online)	1662-8128
ISSN	1662-811X
DOI	10.1159/000525508
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Article ; Online: Previous immunity shapes immune responses to SARS-CoV-2 booster vaccination and Omicron breakthrough infection risk.

Pérez-Alós, Laura / Hansen, Cecilie Bo / Almagro Armenteros, Jose Juan / Madsen, Johannes Roth / Heftdal, Line Dam / Hasselbalch, Rasmus Bo / Pries-Heje, Mia Marie / Bayarri-Olmos, Rafael / Jarlhelt, Ida / Hamm, Sebastian Rask / Møller, Dina Leth / Sørensen, Erik / Ostrowski, Sisse Rye / Frikke-Schmidt, Ruth / Hilsted, Linda Maria / Bundgaard, Henning / Nielsen, Susanne Dam / Iversen, Kasper Karmark / Garred, Peter

Nature communications

2023 Volume 14, Issue 1, Page(s) 5624

Abstract: The heterogeneity of the SARS-CoV-2 immune responses has become considerably more complex over time and diverse immune imprinting is observed in vaccinated individuals. Despite vaccination, following the emergence of the Omicron variant, some individuals ...

Abstract	The heterogeneity of the SARS-CoV-2 immune responses has become considerably more complex over time and diverse immune imprinting is observed in vaccinated individuals. Despite vaccination, following the emergence of the Omicron variant, some individuals appear more susceptible to primary infections and reinfections than others, underscoring the need to elucidate how immune responses are influenced by previous infections and vaccination. IgG, IgA, neutralizing antibodies and T-cell immune responses in 1,325 individuals (955 of which were infection-naive) were investigated before and after three doses of the BNT162b2 vaccine, examining their relation to breakthrough infections and immune imprinting in the context of Omicron. Our study shows that both humoral and cellular responses following vaccination were generally higher after SARS-CoV-2 infection compared to infection-naive. Notably, viral exposure before vaccination was crucial to achieving a robust IgA response. Individuals with lower IgG, IgA, and neutralizing antibody responses postvaccination had a significantly higher risk of reinfection and future Omicron infections. This was not observed for T-cell responses. A primary infection before Omicron and subsequent reinfection with Omicron dampened the humoral and cellular responses compared to a primary Omicron infection, consistent with immune imprinting. These results underscore the significant impact of hybrid immunity for immune responses in general, particularly for IgA responses even after revaccination, and the importance of robust humoral responses in preventing future infections.
MeSH term(s)	Humans ; Breakthrough Infections ; Reinfection ; BNT162 Vaccine ; SARS-CoV-2 ; COVID-19/prevention & control ; Vaccination ; Antibodies, Neutralizing ; Immunity ; Immunoglobulin A ; Immunoglobulin G
Chemical Substances	BNT162 Vaccine ; Antibodies, Neutralizing ; Immunoglobulin A ; Immunoglobulin G
Language	English
Publishing date	2023-09-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-41342-2
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Article ; Online: Lectin Pathway Enzyme MASP-2 and Downstream Complement Activation in COVID-19

Maximilian Peter Götz / Mikkel-Ole Skjoedt / Rafael Bayarri-Olmos / Cecilie Bo Hansen / Laura Pérez-Alós / Ida Jarlhelt / Thomas Benfield / Anne Rosbjerg / Peter Garred

Journal of Innate Immunity, Pp 1-

2022 Volume 14

Abstract	Mannose-binding lectin-associated serine protease 2 (MASP-2) is the main activator of the lectin complement pathway and has been suggested to be involved in the pathophysiology of coronavirus disease 2019 (COVID-19). To study a possible association between MASP-2 and COVID-19, we aimed at developing a sensitive and reliable MASP-2 ELISA. From an array of novel mouse-monoclonal antibodies using recombinant MASP-2 as antigen, two clones were selected to create a sandwich ELISA. Plasma samples were obtained from 216 healthy controls, 347 convalescent COVID-19 patients, and 147 prospectively followed COVID-19 patients. The assay was specific towards MASP-2 and did not recognize the truncated MASP2 splice variant MAP-2 (MAp19). The limit of quantification was shown to be 0.1 ng/mL. MASP-2 concentration was found to be stable after multiple freeze-thaw cycles. In healthy controls, the mean MASP-2 concentration was 524 ng/mL (95% CI: 496.5–551.6). No significant difference was found in the MASP-2 concentrations between COVID-19 convalescent samples and controls. However, a significant increase was observed in prospectively followed COVID-19 patients (mean: 834 ng/mL [95% CI: 765.3–902.7, p < 0.0001]). In these patients, MASP-2 concentration correlated significantly with the concentrations of the terminal complement complex (ρ = 0.3596, p < 0.0001), with the lectin pathway pattern recognition molecules ficolin-2 (ρ = 0.2906, p = 0.0004) and ficolin-3 (ρ = 0.3952, p < 0.0001) and with C-reactive protein (ρ = 0.3292, p = 0.0002). Overall, we developed a specific quantitative MASP-2 sandwich ELISA. MASP-2 correlated with complement activation and inflammatory markers in COVID-19 patients, underscoring a possible role of MASP-2 in COVID-19 pathophysiology.
Keywords	mannose-binding lectin-associated serine protease 2 ; masp-2 ; assay ; covid-19 ; inflammation ; outcome ; Medicine ; R ; Internal medicine ; RC31-1245
Subject code	616
Language	English
Publishing date	2022-07-01T00:00:00Z
Publisher	Karger Publishers
Document type	Article ; Online
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Article: SARS-CoV-2 Natural Antibody Response Persists for at Least 12 Months in a Nationwide Study From the Faroe Islands.

Petersen, Maria Skaalum / Hansen, Cecilie Bo / Kristiansen, Marnar Fríheim / Fjallsbak, Jógvan Páll / Larsen, Sólrun / Hansen, Jóhanna Ljósá / Jarlhelt, Ida / Pérez-Alós, Laura / Steig, Bjarni Á / Christiansen, Debes Hammershaimb / Møller, Lars Fodgaard / Strøm, Marin / Andorsdóttir, Guðrið / Gaini, Shahin / Weihe, Pál / Garred, Peter

Open forum infectious diseases

2021 Volume 8, Issue 8, Page(s) ofab378

Language	English
Publishing date	2021-07-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2757767-3
ISSN	2328-8957
ISSN	2328-8957
DOI	10.1093/ofid/ofab378
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Article ; Online: SARS-CoV-2 Antibodies Mediate Complement and Cellular Driven Inflammation.

Jarlhelt, Ida / Nielsen, Sif Kaas / Jahn, Camilla Xenia Holtermann / Hansen, Cecilie Bo / Pérez-Alós, Laura / Rosbjerg, Anne / Bayarri-Olmos, Rafael / Skjoedt, Mikkel-Ole / Garred, Peter

Frontiers in immunology

2021 Volume 12, Page(s) 767981

Abstract: The ongoing pandemic of coronavirus disease 2019 (COVID-19) caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to constitute a serious public health threat worldwide. Protective antibody-mediated viral neutralization in ... ...

Abstract	The ongoing pandemic of coronavirus disease 2019 (COVID-19) caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to constitute a serious public health threat worldwide. Protective antibody-mediated viral neutralization in response to SARS-CoV-2 infection has been firmly characterized. Where the effects of the antibody response are generally considered to be beneficial, an important biological question regarding potential negative outcomes of a SARS-CoV-2 antibody response has yet to be answered. We determined the distribution of IgG subclasses and complement activation levels in plasma from convalescent individuals using in-house developed ELISAs. The IgG response towards SARS-CoV-2 receptor-binding domain (RBD) after natural infection appeared to be mainly driven by IgG1 and IgG3 subclasses, which are the main ligands for C1q mediated classical complement pathway activation. The deposition of the complement components C4b, C3bc, and TCC as a consequence of SARS-CoV-2 specific antibodies were depending primarily on the SARS-CoV-2 RBD and significantly correlated with both IgG levels and disease severity, indicating that individuals with high levels of IgG and/or severe disease, might have a more prominent complement activation during viral infection. Finally, freshly isolated monocytes and a monocyte cell line (THP-1) were used to address the cellular mediated inflammatory response as a consequence of Fc-gamma receptor engagement by SARS-CoV-2 specific antibodies. Monocytic Fc gamma receptor charging resulted in a significant rise in the secretion of the pro-inflammatory cytokine TNF-α. Our results indicate that SARS-CoV-2 antibodies might drive significant inflammatory responses through the classical complement pathway and
MeSH term(s)	Antibodies, Viral/blood ; COVID-19/blood ; COVID-19/immunology ; Complement Activation ; Complement System Proteins/immunology ; Cytokines/immunology ; Humans ; Immunoglobulin G/blood ; Inflammation/immunology ; Receptors, IgG/immunology ; SARS-CoV-2/immunology ; THP-1 Cells
Chemical Substances	Antibodies, Viral ; Cytokines ; Immunoglobulin G ; Receptors, IgG ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2021-11-02
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2021.767981
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