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ALONSO, S.

Publications and source records attributed to ALONSO, S..

5 recordsLinked to original sources

IFNγ-CXCL9-CXCR3 axis links T cell recruitment to skeletal muscle remodelling in human physical frailty

Introduction: Physical frailty is increasingly prevalent in our ageing society, and results in higher morbidity and healthcare costs. Yet, targeted therapeutics are lacking because underlying mechanisms are poorly defined. Human cohort studies have linked inflammation with frailty, but do not define the mechanisms by which the ageing immune system affects skeletal muscle and physical function. Defining this immune-muscle interaction is therefore crucial for identifying therapeutics for human physical frailty. Methods: We first studied two independent human ageing cohorts (discovery n=22; validation n=33). Physical frailty was quantified with age-adjusted timed-up-and-go (TUG) residuals. Peripheral blood was analysed for plasma OLINK proteomics, high-dimensional spectral immunophenotyping and in a subset, single-cell RNA-sequencing of PBMCs with paired TCR profiling. We then examined an independent human skeletal-muscle cohort (n=340) by bulk RNA-sequencing to derive our proposed immune-muscle axis. Finally, we interrogated individual steps of this axis in primary human in vitro models using IFN{gamma}-conditioned myotube-fibroblast co-cultures, PBMC transwell migration assays with CXCL9 neutralisation (anti-CXCL9) and receptor CXCR3 antagonism (AMG487). Macrophage co-cultured with CD8 were sequentially co-cultured with myotube/fibroblast co-culture, supernatant was then analysed for fibrosis mediators. We used fixed-effect meta-analysis, multivariable models and sequential mediation for analyses. Results: Physical frailty, by single-cell analyses, was associated with a compartmentalised immune-remodelling state involving inflammatory, tissue-remodelling and trafficking programmes in myeloid and T-cells. This finding was validated with plasma proteomics of the same human cohort, where physical frailty was significantly positively associated with an interferon-gamma (IFN{gamma})/CXCR3 (IL-18R1, IFN{gamma}, CXCL9) module, within which plasma CXCL9 was the strongest correlate. CD8-TEMRA and {gamma}{delta} T-cells were most responsive to CXCL9 in physical frailty. This expanded CD8-TEMRA compartment was polyclonal, consistent with bystander IFN{gamma} production rather than a shared antigen-specific response. In human muscle, CXCL9 was significantly positively associated with T-cell module, and through this, fibrosis. Conversely, fibrosis was associated with macrophages. Sequential mediation was consistent with a CXCL9-T-cell-macrophage-fibrosis pathway. Finally, in in-vitro human primary cell experiments, IFN{gamma}-conditioned myotube-fibroblast cultures produced CXCL9 and attracted CD8-TEMRA subsets. Anti-CXCL9 and CXCR3 antagonism significantly reduced this migration, indicating that recruitment of CD8-TEMRA cells was dependent on the CXCL9-CXCR3 axis. Incubating with activated CD8 cells shifted macrophages towards mixed CD163+CD86+ and pro-inflammatory CD163-CD86+ phenotypes. These CD8-co-cultured macrophages in myotube/fibroblast co-culture were associated with increased fibrosis markers transforming growth factor beta-1 and plasminogen activator inhibitor-1. Conclusion: We identified a CD8-TEMRA T-cell migration to human muscle dependent on IFN{gamma}-CXCL9-CXCR3 axis that is associated with human TUG-defined physical frailty which presents potential therapeutic avenues.

immunology↗

Intranasal sarbecovirus vaccine booster elicits cross-clade, durable and protective systemic and mucosal immunity

Short-lived, clade-specific immune responses with limited mucosal priming are limitations faced by current COVID-19 mRNA vaccines against sarbecoviruses. We have developed a nasal booster vaccine candidate that induced robust and sustained, cross-clade, systemic and mucosal protective immunity. Two recombinant Clec9A-specific monoclonal antibodies fused to the Receptor Binding Domain (RBD) from Omicron XBB.1.5 and SARS-CoV-1, respectively were generated. In Comirnaty mRNA-vaccinated mice, boosting with each individual Clec9A-RBD construct induced immune responses that either were limited in breadth or waned over time; while boosting with both constructs combined (Clec9AOMNI) elicited robust cross-clade neutralizing antibodies (nAb) and T cell responses that were significantly more sustained compared to Bivalent Comirnaty (BC) mRNA vaccine booster. The persistence of RBD-specific follicular helper CD4+ T cells, germinal centre B cells, and long-lived plasma cells that facilitated affinity maturation in Clec9AOMNI-boosted mice, correlated with the detection of triple cross-reactive B cells that bind to ancestral SARS-CoV-2 ancestral, SARS-CoV-2 XBB.1.5 and SARS-CoV-1 RBD. Remarkably, intranasal boosting with Clec9AOMNI generated robust and sustained mucosal immune responses in the upper and lower respiratory compartments, including RBD-specific IgA, cross-clade nAb and cellular immunity together with functional tissue-resident memory T cells, without compromising the systemic immune responses. Correspondingly, Clec9AOMNI booster conferred superior protection against Omicron BA.1 compared to BC booster when challenge was performed at six months post-boost. Hence, Clec9AOMNI is a promising nasal booster vaccine candidate that has the potential to mitigate pandemic threats from emerging sarbecoviruses. One Sentence SummaryNasal booster immunization with dendritic cell-targeting vaccine candidate in mRNA-vaccinated mice induced cross-clade, sustained, systemic and mucosal protective immunity.

immunology↗

N153-linked glycans on envelope protein protect orthoflaviviruses from antibody-mediated clearance

The envelope (E) protein of dengue virus (DENV) is glycosylated at two highly conserved asparagine (N) sites (N67 and N153). The role and importance of these N-linked glycans in DENV pathogenesis has been elusive. Here, we report the critical role of N153-linked glycans on E protein in preventing antibody-mediated viral clearance. A DENV2 mutant lacking N153-linked glycans (N153Q mutant) was engineered and found to be mildly impaired in vitro but drastically attenuated in a symptomatic mouse model of severe dengue, as evidenced by accelerated viral clearance. In B cell-deficient mouse models, N153Q mutant displayed parental virulence and viremia profile. Homologous and heterologous passive transfers of purified IgM from infected B cell-proficient mice into B cell-deficient mice demonstrated the role of N153Q-specific IgM in N153Q attenuation and accelerated clearance, while WT DENV was unaffected by IgM from both WT- and N153Q-infected mice. Furthermore, in vitro neutralization assay supported that the accelerated clearance of N153Q mutant in mice was mediated by non-neutralizing IgM. Furthermore, using plasma samples from convalescent dengue patients and monoclonal antibodies, in vitro neutralization assays showed that N153Q virus was more susceptible than WT to IgG-mediated neutralization. Glycoproteomics combined with molecular dynamics (MD) simulations revealed that glycan composition on E protein influenced IgG binding. Our findings were extended to all DENV serotypes and ZIKV, hence supporting that the N153 glycans-mediated immune evasion strategy is conserved across orthoflaviviruses.

microbiology↗

De-glycosylated non-structural protein 1 enhances dengue virus clearance by limiting PD-L1/PD-1 mediated T cell apoptosis

The non-structural protein 1 (NS1) of dengue virus (DENV) contains two highly conserved N-glycosylation sites at positions 130 and 207 (N130 and N207). Intracellular NS1 monomers and homo-dimers participate in viral RNA replication within membrane-bound replication complexes. Soluble multimeric NS1 (sNS1) is secreted into the extracellular milieu and represents an important virulence factor for DENV through its ability to interfere with the host complement activation cascade and to induce vascular leakage. The role of the two N-glycans in NS1 biological activities, however, has not been carefully examined. Here, stable DENV2 mutants that lack glycan at either N sites of NS1 were engineered. We showed that the lack of glycans at either N site of NS1 did not impair viral replication nor viral output in both mosquito and mammalian cell lines. In contrast, while N130 de-glycosylated DENV displayed parental in vivo fitness in IFNAR-/- mice, the N207 de-glycosylated mutant was significantly attenuated as evidenced by 100% survival rate, which correlated with accelerated viral clearance in circulation. sNS1-depletion, sNS1 exogenous administration and co-infection experiments supported that N207 de-glycosylated NS1 exerted a dominant attenuating effect during in vivo infection. Bulk RNAseq, inflammatory cytokine profile, immune phenotyping of neutrophils and T cells, immune cell depletion and immune checkpoint blockade approaches led us to propose that N207 de-glycosylated NS1 limited CD8+ T cell apoptosis mediated by the PD-L1/PD-1 axis, thereby improving viral clearance efficacy. This work uncovers a novel immune evasion strategy where N207 glycans on NS1 prevent the protein from exerting immune modulation activity that would be detrimental to DENV.

microbiology↗

Relative contribution of non-structural protein 1 in dengue pathogenesis

Dengue is a major public health concern in the tropical and sub-tropical world with no effective treatment. The controversial live attenuated virus vaccine Dengvaxia has boosted the pursuit of sub-unit vaccine approaches, and the non-structural protein 1 (NS1) has recently emerged as a promising candidate. However, we found that NS1 immunization or passive transfer of NS1 antibodies failed to confer protection in symptomatic dengue mouse models using two non mouse-adapted DENV2 strains from the Cosmopolitan genotype that currently circulates in South-East Asia. Furthermore, exogenous administration of purified NS1 did not worsen in vivo vascular leakage in sub-lethally infected mice, thereby supporting that NS1 does not play a critical role in the pathogenesis of these DENV2 strains. Virus chimerization approaches indicated that the prME structural region, but not NS1, plays a critical role in driving in vivo fitness and virulence of the virus, through induction of key pro-inflammatory cytokines. This work highlights that the pathogenic role of NS1 is DENV strain-dependent, which warrants re-evaluation of NS1 as a universal dengue vaccine candidate.

microbiology↗