Evidence map›Paper›PMID 41889643›Full record

ArticleFrontiers in microbiology2026

Unraveling the dual immunomodulatory and immunogenic roles of the central conserved cysteine-rich region in respiratory syncytial virus G protein.

Juan Gutman, Ana Luz Paletta, Federico Birnberg-Weiss, Cecilia Arahi Prato, Analía Boudgouste, Carla Jimena Goldin, Santiago Sastre, Alana Brooke Byrne, Pablo Pakciarz, Fernando Pedro Polack and 8 more

Abstract read
In one paragraph

Article in Frontiers in microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

18 authors.

Juan GutmanCentro de Rediseño e Ingeniería de Proteínas (CRIP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Ana Luz PalettaInstituto de Investigaciones Biotecnológicas (IIBio), CONICET, Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Federico Birnberg-WeissLaboratorio de Fisiología de los Procesos Inflamatorios, Instituto de Medicina Experimental (IMEX)-CONICET, Academia Nacional de Medicina, Buenos Aires, Argentina.
Cecilia Arahi PratoInstituto de Investigaciones Biotecnológicas (IIBio), CONICET, Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Analía BoudgousteCentro de Rediseño e Ingeniería de Proteínas (CRIP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Carla Jimena GoldinCentro de Rediseño e Ingeniería de Proteínas (CRIP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Santiago SastreDepartamento de Biofísica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay.
Alana Brooke ByrneCentro de Rediseño e Ingeniería de Proteínas (CRIP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Pablo PakciarzCentro Infant de Medicina Traslacional (CIMeT), Escuela de Bio y Nanotecnología, Universidad Nacional de San Martín, Buenos Aires, Argentina.
Fernando Pedro PolackFundación INFANT, Buenos Aires, Argentina.
Julia DvorkinCentro Infant de Medicina Traslacional (CIMeT), Escuela de Bio y Nanotecnología, Universidad Nacional de San Martín, Buenos Aires, Argentina.
Ari ZeidaCentro de Investigaciones Biomédicas (CEINBIO), Facultad de Medicina, Universidad de la República, Montevideo, Uruguay.
Mauricio Tomas CaballeroCentro Infant de Medicina Traslacional (CIMeT), Escuela de Bio y Nanotecnología, Universidad Nacional de San Martín, Buenos Aires, Argentina.
Verónica Inés LandoniLaboratorio de Fisiología de los Procesos Inflamatorios, Instituto de Medicina Experimental (IMEX)-CONICET, Academia Nacional de Medicina, Buenos Aires, Argentina.
Gabriela Cristina FernándezLaboratorio de Fisiología de los Procesos Inflamatorios, Instituto de Medicina Experimental (IMEX)-CONICET, Academia Nacional de Medicina, Buenos Aires, Argentina.
María Virginia TribulattiInstituto de Investigaciones Biotecnológicas (IIBio), CONICET, Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Damian Alvarez-PaggiCentro de Rediseño e Ingeniería de Proteínas (CRIP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.
Sebastián Andrés EsperanteCentro de Rediseño e Ingeniería de Proteínas (CRIP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Escuela de Bio y Nanotecnologías (EByN), Universidad Nacional de San Martín (UNSAM), Buenos Aires, Argentina.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Respiratory syncytial virus (RSV) causes severe respiratory disease in infants and high-risk adults, in part by subverting host immunity. The RSV G glycoprotein's central conserved cysteine rich domain (CCD) contains a CX3C motif implicated in immune modulation, but the relationship between its redox state, structural conformation, and immune modulatory function remains unclear. Methods: In this study, we recombinantly expressed a CCD-derived peptide (Gpep, residues 149-196), determined its redox-dependent folding by reversed-phase HPLC (RP-HPLC) and biophysical analyses, and assessed its function using murine dendritic cell and human neutrophil assays alongside pediatric serology. Results: Kinetic analyses by RP‑HPLC and biophysical techniques showed that reduced Gpep rapidly folds through a predominant intermediate to yield an oxidized monomer; conversely, higher concentrations drive intermolecular disulfide isomerization and covalent oligomer formation. Functionally, Gpep inhibited dendritic cell activation elicited by both LPS- and UV-inactivated RSV. In addition, Gpep suppressed multiple human neutrophil responses, including chemotaxis, CD11b upregulation, reactive oxygen species production, myeloperoxidase release, and NET formation, without inducing cytotoxicity. In contrast, oligomerized Gpep lacked immunosuppressive activity. Serological analysis of an ambulatory pediatric cohort (0-72 months) showed a transient increase in the anti-F/anti-G IgG ratio following early RSV exposures, consistent with preferential maturation of F-directed responses. Discussion: We propose a redox‑dependent immune‑evasion model in which secreted, monomeric G mediates transient immunosuppression that is halted by disulfide‑driven oligomerization of membrane‑bound G and F proteins. These findings support a mechanistic association between the redox state of RSV G, its oligomeric behavior, and its immunomodulatory properties.

Indexed as

host/pathogen interactionsimmunomodulationimmunopathogenesisredoxRSVG central conserved domain

Identifiers

PMID41889643
PMCPMC13013481

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