Cuban Abdala vaccine: Effectiveness in preventing severe disease and death from COVID-19 in Havana, Cuba; A cohort study

Más-Bermejo, Pedro I.; Dickinson-Meneses, Félix O.; Almenares-Rodríguez, Kenia; Sánchez, Lizet; Guinovart-Dı́az, Raúl; Vidal-Ledo, María; Galbán-García, Enrique; Olivera-Nodarse, Yadira; Morgado-Vega, Isabel; Dueñas‐Carrera, Santiago; Pujol, Merardo; Hernández-Bernal, Francisco; Limonta-Fernández, Miladys; Guillén-Nieto, Gerardo; Muzio-González, Verena L.; Ayala-Ávila, Marta

doi:10.1016/j.lana.2022.100366

Cited by 24 publications

(16 citation statements)

References 19 publications

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“…Evidence from the deployment of the vaccine also suggests that it is highly effective. A retrospective cohort study conducted between May and August 2021 evaluated public health data from over a million people in the city of Havana and found that the real-world effectiveness of the vaccine met or exceeded estimates of VE during the trial, with 98.2% effectiveness against severe disease and 98.7% effectiveness against death observed in fully vaccinated subjects ( 218 ). Notably, Cuba has vaccinated a high percentage of its population, with 87% of the population vaccinated by January 2022 and 90.3% by the end of December 2022 ( 219 , 220 ).…”

Section: Subunit Vaccinesmentioning

confidence: 99%

Application of Traditional Vaccine Development Strategies to SARS-CoV-2

et al. 2023

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Section: Subunit Vaccinesmentioning

confidence: 99%

Application of Traditional Vaccine Development Strategies to SARS-CoV-2

et al. 2023

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“…Finally, the results from this work point to the importance of understanding the impact of N- glycosylation in protein structure and stability, with immediate consequences to COVID-19 vaccine design. Indeed, earlier work shows SARS-CoV-2 S-based protein vaccines with increased efficacy due to the removal of N -glycans(Huang et al, 2022), and of RBD-based vaccines in use and under development(Cohen et al, 2022; Más-Bermejo et al, 2022; Valdes-Balbin et al, 2021) that may be designed with and without N- glycans. The design of such constructs may benefit from understanding which N- glycosylation sites are structurally essential and which are dispensable.…”

Section: Discussionmentioning

confidence: 99%

#GotGlycans: Role of N343 Glycosylation on the SARS-CoV-2 S RBD Structure and Co-Receptor Binding Across Variants of Concern

Ives,

Nguyen,

Fogarty

et al. 2023

Preprint

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Glycosylation of the SARS-CoV-2 spike (S) protein represents a key target for viral evolution because it affects both viral evasion and fitness. Successful variations in the glycan shield are difficult to achieve though, as protein glycosylation is also critical to folding and to structural stability. Within this framework, the identification of glycosylation sites that are structurally dispensable can provide insight into the evolutionary mechanisms of the shield and inform immune surveillance. In this work we show through over 45 μs of cumulative sampling from conventional and enhanced molecular dynamics (MD) simulations, how the structure of the immunodominant S receptor binding domain (RBD) is regulated byN-glycosylation at N343 and how this glycan’s structural role changes from WHu-1, alpha (B.1.1.7), and beta (B.1.351), to the delta (B.1.617.2) and omicron (BA.1 and BA.2.86) variants. More specifically, we find that the amphipathic nature of theN-glycan is instrumental to preserve the structural integrity of the RBD hydrophobic core and that loss of glycosylation at N343 triggers a specific and consistent conformational change. We show how this change allosterically regulates the conformation of the receptor binding motif (RBM) in the WHu-1, alpha and beta RBDs, but not in the delta and omicron variants, due to mutations that reinforce the RBD architecture. In support of these findings, we show that the binding of the RBD to monosialylated ganglioside co-receptors is highly dependent on N343 glycosylation in the WHu-1, but not in the delta RBD, and that affinity changes significantly across VoCs. Ultimately, the molecular and functional insight we provide in this work reinforces our understanding of the role of glycosylation in protein structure and function and it also allows us to identify the structural constraints within which the glycosylation site at N343 can become a hotspot for mutations in the SARS-CoV-2 S glycan shield.

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“…The majority of them were developed in central countries and resulted in several approaches that were distributed worldwide. However, peripheral countries, like Argentina, Brazil, Cuba, and India, have also made their own developments providing resources to local production necessary to fight against this respiratory disease ( 4 , 5 ). 1 , 2 One of these initiatives was the Argentinean AntiCovid Consortium, where we partnered with nearly 30 researchers (PIs, young researchers, postdocs and PhD students) from different scientific backgrounds, combining our knowledge and expertise to carry out a multidisciplinary strategy.…”

Section: Introductionmentioning

confidence: 99%

Policy options and practical recommendations for determining priorities in public health research agendas in peripheral countries: insights from a collaborative work initiative in Argentina during the COVID-19 pandemic

Fernández,

Herrera,

Blaustein

et al. 2024

Front. Med.

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Cuban Abdala vaccine: Effectiveness in preventing severe disease and death from COVID-19 in Havana, Cuba; A cohort study

Cited by 24 publications

References 19 publications

Application of Traditional Vaccine Development Strategies to SARS-CoV-2

Application of Traditional Vaccine Development Strategies to SARS-CoV-2

#GotGlycans: Role of N343 Glycosylation on the SARS-CoV-2 S RBD Structure and Co-Receptor Binding Across Variants of Concern

Policy options and practical recommendations for determining priorities in public health research agendas in peripheral countries: insights from a collaborative work initiative in Argentina during the COVID-19 pandemic

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