scholarly journals T-Cell Epitopes in Severe Acute Respiratory Syndrome (SARS) Coronavirus Spike Protein Elicit a Specific T-Cell Immune Response in Patients Who Recover from SARS

2004 ◽  
Vol 78 (11) ◽  
pp. 5612-5618 ◽  
Author(s):  
Yue-Dan Wang ◽  
Wan-Yee Fion Sin ◽  
Guo-Bing Xu ◽  
Huang-Hua Yang ◽  
Tin-yau Wong ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Epitope ◽  
T Cell Response ◽  
Cell Immune Response ◽  
T Cell Epitopes ◽  
Online Database ◽  
Database Analysis ◽  
S Protein ◽  
Healthy Donors ◽  
Ifn Γ

ABSTRACT The immunogenicity of HLA-A2-restricted T-cell epitopes in the S protein of the Severe acute respiratory syndrome coronavirus (SARS-CoV) and of human coronavirus strain 229e (HCoV-229e) was analyzed for the elicitation of a T-cell immune response in donors who had fully recovered from SARS-CoV infection. We employed online database analysis to compare the differences in the amino acid sequences of the homologous T epitopes of HCoV-229e and SARS-CoV. The identified T-cell epitope peptides were synthesized, and their binding affinities for HLA-A2 were validated and compared in the T2 cell system. The immunogenicity of all these peptides was assessed by using T cells obtained from donors who had fully recovered from SARS-CoV infection and from healthy donors with no history of SARS-CoV infection. HLA-A2 typing by indirect immunofluorescent antibody staining showed that 51.6% of SARS-CoV-infected patients were HLA-A2 positive. Online database analysis and the T2 cell binding test disclosed that the number of HLA-A2-restricted immunogenic epitopes of the S protein of SARS-CoV was decreased or even lost in comparison with the homologous sequences of the S protein of HCoV-229e. Among the peptides used in the study, the affinity of peptides from HCoV-229e (H77 and H881) and peptides from SARS-CoV (S978 and S1203) for binding to HLA-A2 was higher than that of other sequences. The gamma interferon (IFN-γ) release Elispot assay revealed that only SARS-CoV-specific peptides S1203 and S978 induced a high frequency of IFN-γ-secreting T-cell response in HLA-A2+ donors who had fully recovered from SARS-CoV infection; such a T-cell epitope-specific response was not observed in HLA-A2+ healthy donors or in HLA-A2− donors who had been infected with SARS-CoV after full recovery. Thus, T-cell epitopes S1203 and S978 are immunogenic and elicit an overt specific T-cell response in HLA-A2+ SARS-CoV-infected patients.

scholarly journals Immunodominance in Mouse and Human CD4+ T-Cell Responses Specific for the Bordetella pertussis Virulence Factor P.69 Pertactin

2008 ◽  
Vol 77 (2) ◽  
pp. 896-903 ◽  
Author(s):  
Rachel M. Stenger ◽  
Martien C. M. Poelen ◽  
Ed E. Moret ◽  
Betsy Kuipers ◽  
Sven C. M. Bruijns ◽  
...  
Keyword(s):  
T Cell ◽  
Bordetella Pertussis ◽  
Cell Epitope ◽  
T Cell Response ◽  
T Cell Epitopes ◽  
Cell Responses ◽  
Cell Immunity ◽  
Hla Dq ◽  
Natural Variants ◽  
Acellular Vaccines

ABSTRACT P.69 pertactin (P.69 Prn), an adhesion molecule from the causative agent of pertussis, Bordetella pertussis, is present in cellular and most acellular vaccines that are currently used worldwide. Although both humoral immunity and cellular immunity directed against P.69 Prn have been implicated in protective immune mechanisms, the identities of CD4+ T-cell epitopes on the P.69 Prn protein remain unknown. Here, a single I-Ad-restricted B. pertussis conserved CD4+ T-cell epitope at the N terminus of P.69 Prn was identified by using a BALB/c T-cell hybridoma. The epitope appeared immunodominant among four other minor strain-conserved P.69 Prn epitopes recognized after vaccination and B. pertussis infection, and it was capable of evoking a Th1/Th17-type cytokine response. B. pertussis P.69 Prn immune splenocytes did not cross-react with natural variants of the epitope as present in Bordetella parapertussis and Bordetella bronchiseptica. Finally, it was found that the immunodominant P.69 Prn epitope is broadly recognized in the human population by CD4+ T cells in an HLA-DQ-restricted manner. During B. pertussis infection, the epitope was associated with a Th1-type CD4+ T-cell response. Hence, this novel P.69 Prn epitope is involved in CD4+ T-cell immunity after B. pertussis vaccination and infection in mice and, more importantly, in humans. Thus, it may provide a useful tool for the evaluation of the type, magnitude, and maintenance of B. pertussis-specific CD4+ T-cell mechanisms in preclinical and clinical vaccine studies.

The CD4+ T-cell response to adenovirus is focused against conserved residues within the hexon protein

2007 ◽  
Vol 88 (9) ◽  
pp. 2417-2425 ◽  
Author(s):  
David Onion ◽  
Laura J. Crompton ◽  
Donald W. Milligan ◽  
Paul A. H. Moss ◽  
Steven P. Lee ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Cell Response ◽  
Protein A ◽  
T Cell Response ◽  
Cd4 T Cell ◽  
T Cell Epitopes ◽  
Hexon Protein ◽  
Healthy Donors ◽  
Fiber Proteins

Adenovirus is a significant pathogen in immunocompromised patients and is widely utilized as a gene delivery vector, so a detailed understanding of the human immune response to adenovirus infection is critical. This study characterized the adenovirus-specific CD4+ T-cell response of healthy donors by incubation with whole virus or with individual hexon and fiber proteins. Adenovirus-specific CD4+ T cells averaged 0.26 % of the CD4+ T-cell pool and were detectable in all donors. T cells recognizing the highly conserved hexon protein accounted for 0.09 %, whereas no response was observed against the fiber protein. A panel of hexon-specific CD4+ T-cell clones was generated and shown to lyse targets infected with adenovirus from different serotypes and species. Three CD4 T-cell epitopes are described, which map to highly conserved regions of the hexon protein.

Identification of the AAV2 Capsid CD8+ T Cell Epitope in C57BL/6 Mice.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 3188-3188
Author(s):  
Denise E. Sabatino ◽  
Federico Mingozzi ◽  
Haifeng Chen ◽  
Peter Colosi ◽  
Hildegund C.J. Ertl ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Immune Responses ◽  
Capsid Protein ◽  
Cd8 T Cells ◽  
Cell Epitope ◽  
T Cell Response ◽  
Cd8 Cells ◽  
Media Control ◽  
Ifn Γ

Abstract Recently, a clinical trial for adeno-associated virus serotype 2 (AAV2) mediated liver directed gene transfer of human Factor IX to subjects with severe hemophilia B revealed that two patients developed transient asymptomatic transaminitis following vector administration. Immunology studies in the second patient demonstrated a transient T cell response to AAV2 capsid peptides suggesting that the immune response to the AAV capsid may be related to the transient transaminitis. We hypothesized that the observations made in the human subjects were due to a CD8 T cell response to AAV2 capsid protein. Preclinical studies in mice and dogs, which are not naturally infected by wild type AAV2 viruses, did not predict these findings in the clinical study. Thus, we developed a mouse model in which we were able to mimic this phenomenon (Blood 102:493a). In an effort to further characterize the immune responses to AAV2 capsid proteins in this mouse model, we identified the T cell epitope in the AAV capsid protein recognized by murine C57Bl/6 CD8 T cells. A peptide library of AAV2 VP1 capsid peptides (n=145) that were synthesized as 15mers overlapping by 10 amino acids were divided into 6 pools each containing 24–25 peptides. C57Bl/6 mice were immunized intramuscularly with an adenovirus expressing AAV2 capsid protein. Nine days later the spleen was harvested and intracellular cytokine staining (ICS) was used to assess release of IFN-γ from CD8 T cells in response to 6 AAV2 capsid peptide pools. ICS demonstrated CD8 cells from mice immunized with Ad-AAV2 produced IFN-γ (3.5% of the CD8 cells) in response to Pool F (amino acid 119–145) while no IFN-γ release in CD8 cells was detected with Pool A to E (mean 0.28%±0.25%) compared to the media control (0.16%). This detection of IFN-γ release from CD8 T cells indicates a specific proliferation to a peptide(s) within this peptide pool (Pool F). A matrix approach was used to further define which peptide(s) contained the immunodominant epitope. Eleven small peptide pools of Pool F were created in which each peptide was represented in 2 pools. ICS of splenocytes from immunized (Ad-AAV2 capsid) C57Bl/6 mice demonstrated IFN-γ response from CD8 cells to 3 of the matrix pools corresponding to peptide 140 (PEIQYTSNYNKSVNV) and 141 (TSNYNKSVNVDFTVD) compared with media controls. To determine the exact peptide sequence that binds to the MHC Class I molecule, 9 amino acid peptides (n=7) were created that overlap peptide 140 and 141. Peptide SNYNKSVNV showed positive staining for both CD8 and IFN- γ(3.2%) compared with the six other peptides (0.14%±0.08%), media control (0.08%) and mice that were not immunized (0.11%). This epitope lies in the C terminus of the AAV2 VP1 capsid protein. Current studies using strains of mice with different MHC H2 haplotypes will allow us to determine which of the C57Bl/6 MHC alleles the epitope binds. These findings will provide us with a powerful tool for assessing immune responses to AAV capsid in the context of gene therapy. Specifically, they will allow us to determine how long immunologically detectable capsid sequences persist in an animal injected with AAV vectors. This in turn will provide a basis for a clinical study in which subjects are transiently immunosuppressed, from the time of vector injection until capsid epitopes are no longer detectable by the immune system.

CD4 T-Helper Responses to the ALK Protein in Patients with ALK-Positive ALCL.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 3352-3352
Author(s):  
Kamel K. Ait-Tahar ◽  
Chris S.R. Hatton ◽  
Karen K. Pulford
Keyword(s):  
T Cell ◽  
T Cell Response ◽  
Cytotoxic T Cell ◽  
Immune Recognition ◽  
T Helper ◽  
Healthy Donors ◽  
Irrelevant Peptide ◽  
Ifn Γ ◽  
Alk Positive ◽  
Alk Protein

Abstract Anaplstic Lymphoma Kinase (ALK)-positive anaplastic large cell lymphoma (ALCL) has a favourable prognostic outlook compared to ALK-negative AlCL, possibly as a result of the immune recognition of the ALK protein. We have previously shown the presence of both a cytotoxic T cell and an antibody response to the ALK protein in patients with ALK-positive ALCL. The aim of our present study was to investigate the presence of a CD4 T-helper (Th) response in patients with ALK-positive ALCL and in control individuals. Using the TEPITOPE web-based predicitive search algorithm, three 24-mer promiscuous peptides were identified from the ALK sequence as being potentially immunogenic in the context of MHC class II. A gamma-interferon (γ-IFN) and IL-4 ELISPOT assay was used to detect a T cell response in the peripheral blood cells from patients with ALK-positive and ALK- negative ALCL, as well as healthy controls after 6–11 days of culture with the three peptides. ALK278–301 and ALK233–256 were shown to be highly immunogenic in the majority of the ALK-positive patients (see Table). ALK411–434 was immunogenic to T cells from only one of the ALK-positive patients (Patient 4). Cells from none of the two ALK-negative ALCL patients or the five healthy donors showed any reactivity to the ALK peptides. No response to the control irrelevant peptide was observed in any of the ALCL patients or healthy donors. With the exception of one ALK-positive ALCL patient (Patient 2), no significant IL-4 response was recorded in any of the patients or controls. All of the ALK-positive patients presented antibodies to the ALK protein at time of diagnosis.These findings further demonstrate the immunogenicity of the ALK protein and are suggestive of a Th1 type of immune response to the protein. Our findings are of potential prognostic value and open up therapeutic options for those ALK-positive patients who do not respond well to chemotherapy. Summary of the CD4 Th responses to ALK in ALCL patients and healthy donors None PHA (10 μ g/ml) ALK233–256 (10 μM)- (IFN- γ/IL-4) ALK278–301(10 μM)- (IFN- γ/IL-4) ALK411–434 (10 μM)- (IFN- γ/IL-4) Irrelevant peptide (10 μM)- (IFN- γ) Antibody titres to ALK (IgG isotype) ND= Not done. Results are of triplicate cultures ALK+ve patients Patient 1 12 188 56/10 44/18 22/6 8 1/2250 Patient 2 20 240 126/48 78/52 40/26 18 1/2250 Patient 3 14 48 38/ND 24/ND 12/ND 16 1/6750 Patient 4 6 108 64/8 72/8 22/6 10 1/60750 Patient 5 10 48 36/13 26/18 12/12 14 1/6750 Patient 6 15 132 74/ND 58/ND 28/ND 18 1/6750 Patient 7 10 180 34/28 56/32 12/9 12 1/750 ALK-ve patients Patient 8 14 122 12/10 10/6 12/14 22 −ve Patient 9 16 82 14/ND 12/ND 10/ND 24 −ve Healthy Donors Normal 1 22 148 18/14 22/24 26/12 10 −ve Normal 2 12 18 2/4 6/8 12/2 4 −ve Normal 3 10 38 12/10 12/16 9/4 18 −ve Normal 4 9 172 9/ND 10/ND 6/ND 12 −ve Normal 5 4 108 8/12 8/12 2/1 10 −ve

scholarly journals Screening of HLA-A restricted T cell epitopes of SARS-CoV-2 and induction of CD8+ T cell responses in HLA-A transgenic mice

2021 ◽  
Author(s):  
Xiaoxiao Jin ◽  
Ding Yan ◽  
Sun Shihui ◽  
Xinyi Wang ◽  
Zining Zhou ◽  
...  
Keyword(s):  
T Cell ◽  
Transgenic Mice ◽  
Cell Epitope ◽  
T Cell Responses ◽  
Poly I:C ◽  
T Cell Epitopes ◽  
Cell Responses ◽  
Mhc Class I Molecule ◽  
Healthy Donors ◽  
Epitope Vaccines

AbstractWhile SARS-CoV-2-specific T cells have been characterized to play essential roles in host immune protection in COVID-19 patients, few researches focus on the functional validation of T cell epitopes and development of vaccines inducing specific T cell responses. In this study, 120 CD8+ T cell epitopes from E, M, N, S and RdRp proteins of SARS-CoV-2 were validated by on-silicon prediction, DC-peptide-PBL costimulation with healthy donors’ PBMCs and HLA-A molecule competitive binding experiments. Among them, 110, 15, 6, 14 and 12 epitopes were highly homologous with SARS-CoV, OC43, NL63, HKU1, and 229E, respectively. Thirty-one epitopes restricted by HLA-A2 molecule were used to generate peptide cocktail vaccines in combination with Poly(I:C), R848 or polylactic-co-glycolic acid nanoparticles, which elicited robust specific CD8+ T cell responses in wild-type and HLA-A2/DR1 transgenic mice. Seven of the 31 epitopes were found to be cross-presented by HLA-A2 and H-2K/Db molecules. These data have provided a library of SARS-CoV-2 CD8+ T cell epitopes which restricted by a series of high-frequency HLA-A allotypes and covered broad population in Asia, and initially confirmed the feasibility of human MHC class I molecule-restricted SARS-CoV2 epitope peptide cocktail vaccines, thus will facilitate the development of T cell epitope vaccines and specific cellular function detection kits.

scholarly journals Introduction of Non-natural Amino Acids Into T-Cell Epitopes to Mitigate Peptide-Specific T-Cell Responses

2021 ◽  
Vol 12 ◽  
Author(s):  
Aurélien Azam ◽  
Sergio Mallart ◽  
Stephane Illiano ◽  
Olivier Duclos ◽  
Catherine Prades ◽  
...  
Keyword(s):  
Amino Acids ◽  
T Cells ◽  
T Cell ◽  
T Cell Activation ◽  
Cell Activation ◽  
Cell Epitope ◽  
T Cell Response ◽  
T Cell Epitopes ◽  
Anchor Residue ◽  
Hla Dr

Non-natural modifications are widely introduced into peptides to improve their therapeutic efficacy, but their impact on immunogenicity remains largely unknown. As the CD4 T-cell response is a key factor in triggering immunogenicity, we investigated the effect of introducing D-amino acids (Daa), amino isobutyric acid (Aib), N-methylation, Cα-methylation, reduced amide, and peptoid bonds into an immunoprevalent T-cell epitope on binding to a set of HLA-DR molecules, recognition, and priming of human T cells. Modifications are differentially accepted at multiple positions, but are all tolerated in the flanking regions. Introduction of Aib and Daa in the binding core had the most deleterious effect on binding to HLA-DR molecules and T-cell activation. Their introduction at the positions close to the P1 anchor residue abolished T-cell priming, suggesting they might be sufficient to dampen peptide immunogenicity. Other modifications led to variable effects on binding to HLA-DR molecules and T-cell reactivity, but none exhibited an increased ability to stimulate T cells. Altogether, non-natural modifications appear generally to diminish binding to HLA-DR molecules and hence T-cell stimulation. These data might guide the design of therapeutic peptides to make them less immunogenic.

scholarly journals Antigenicity of peptides comprising the immunosuppressive domain of the retroviral envelope glycoprotein

2017 ◽  
Vol 1 ◽  
pp. 22
Author(s):  
Bryony Jenkins ◽  
Urszula Eksmond ◽  
George Young ◽  
George Kassiotis
Keyword(s):  
T Cell ◽  
Envelope Glycoprotein ◽  
Cell Epitope ◽  
Lymphocyte Activation ◽  
T Cell Response ◽  
Antigenic Peptides ◽  
T Cell Epitopes ◽  
Immunosuppressive Activity ◽  
Histocompatibility Complex ◽  
Antigenic Epitopes

To achieve persistent infection of the host, viruses often subvert or suppress host immunity through mechanisms that are not entirely understood. The envelope glycoprotein of several retroviruses is thought to possess potent immunosuppressive activity, mapped to a 17-amino acid residue conserved domain. Synthetic peptides corresponding to this immunosuppressive domain can inhibit lymphocyte activation, whereas mutation of key domain residues can increase the lymphocyte response to linked antigenic epitopes. Using three T cell receptors (TCRs) of defined specificity, we examine the effect of the immunosuppressive domain on the T cell response to their respective antigenic peptides. We find that fusion of a T cell epitope to the immunosuppressive domain can greatly modulate its potency. However, the effects heavily depend on the particular combination of TCR and peptide-major histocompatibility complex class II (pMHC II), and are mimicked by sequence-scrambled peptides of similar length, suggesting they operate at the level of pMHC formation or TCR-pMHC interaction. These results offer an alternative explanation for the immunogenicity of T cell epitopes comprising the putative immunosuppressive domain, which is more consistent with an effect on peptide antigenicity than true immunosuppressive activity.

scholarly journals Antigenicity of peptides comprising the immunosuppressive domain of the retroviral envelope glycoprotein

2016 ◽  
Vol 1 ◽  
pp. 22
Author(s):  
Bryony Jenkins ◽  
Urszula Eksmond ◽  
George Young ◽  
George Kassiotis
Keyword(s):  
T Cell ◽  
Envelope Glycoprotein ◽  
Cell Epitope ◽  
Lymphocyte Activation ◽  
T Cell Response ◽  
Antigenic Peptides ◽  
T Cell Epitopes ◽  
Immunosuppressive Activity ◽  
Histocompatibility Complex ◽  
Antigenic Epitopes

To achieve persistent infection of the host, viruses often subvert or suppress host immunity through mechanisms that are not entirely understood. The envelope glycoprotein of several retroviruses is thought to possess potent immunosuppressive activity, mapped to a 17-amino acid residue conserved domain. Synthetic peptides corresponding to this immunosuppressive domain can inhibit lymphocyte activation, whereas mutation of key domain residues can increase the lymphocyte response to linked antigenic epitopes. Using three T cell receptors (TCRs) of defined specificity, we examine the effect of the immunosuppressive domain on the T cell response to their respective antigenic peptides. We find that fusion of a T cell epitope to the immunosuppressive domain can greatly modulate its potency. However, the effects heavily depend on the particular combination of TCR and peptide-major histocompatibility complex class II (pMHC II), and are mimicked by sequence-scrambled peptides of similar length, suggesting they operate at the level of TCR-pMHC interaction. These results offer an alternative explanation for the immunogenicity of T cell epitopes comprising the putative immunosuppressive domain, which is more consistent with an effect on peptide antigenicity than true immunosuppressive activity.

scholarly journals SARS-CoV-2 Spike Protein Evolution may Cause Difficulties for Vaccine

2020 ◽  
Author(s):  
Jian Zhou ◽  
Sun Jingjing ◽  
Gang Lu ◽  
Wanchun Wang ◽  
Lin Wang
Keyword(s):  
T Cell ◽  
B Cell ◽  
3D Model ◽  
Bioinformatics Analysis ◽  
Cell Epitope ◽  
Amino Acid Sequences ◽  
T Cell Epitopes ◽  
Sequence Structure ◽  
B Cell Epitopes ◽  
S Protein

Abstract Background: Coronavirus disease 2019 (COVID-19) poses a great threat to human health and life. We performed a bioinformatics analysis to compare the sequence, structure, and epitopes of SARS-CoV-2 spike (S) protein in 10 different countries. Methods: The amino acid sequences of SARS-CoV-2 S protein were obtained from the NCBI database. We used DNASTAR Lasergene software to analyze the protein’s secondary structures. SWISS-MODEL combined with VMD software was used to construct a 3D model of SARS-CoV-2 S protein. DNASTAR Protean and the IEDB database were used to analyze the B cell epitopes and T cell epitopes, respectively. Results: The results of B cell epitopes analysis indicated that the epitopes of SARS-CoV-2 S protein in Korea and American increased, which suggested that the antigenicity of SARS-CoV-2 in Czech, Korea and American might be enhanced. A small number of B cell epitopes disappeared in the SARS-CoV-2 S protein sequence from Greece, Australia, Sweden and India, which suggested that the antigenicity of SARS-CoV-2 in Greece, Australia, Sweden and India may be weakened. T cell epitope analysis indicated that the antigenicity of SARS-CoV-2 in Czech, Korea and American was enhanced, while antigenicity of SARS-CoV-2 in Greece, Australia, Inida, Sweden and Thailand may be weakened. The sequence of SARS-CoV-2 S protein has changed as the virus has spread, and the structures and epitopes have changed accordingly. Conclusion: The mutation leads to a decrease in the antigenicity of SARS-CoV-2, which may be a mechanism for the virus to evade surveillance by the immune system.

scholarly journals Degenerate CD8 Epitopes Mapping to Structurally Constrained Regions of the Spike Protein: A T Cell-Based Way-Out From the SARS-CoV-2 Variants Storm

2021 ◽  
Vol 12 ◽  
Author(s):  
Carolina Boni ◽  
Davide Cavazzini ◽  
Angelo Bolchi ◽  
Marzia Rossi ◽  
Andrea Vecchi ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Epitope ◽  
Cd8 T Cell ◽  
T Cell Response ◽  
Viral Escape ◽  
Cell Mediated Immunity ◽  
Structural Constraints ◽  
T Cell Epitopes ◽  
Cell Responses ◽  
Hla Class I Molecules

There is an urgent need for new generation anti-SARS-Cov-2 vaccines in order to increase the efficacy of immunization and its broadness of protection against viral variants that are continuously arising and spreading. The effect of variants on protective immunity afforded by vaccination has been mostly analyzed with regard to B cell responses. This analysis revealed variable levels of cross-neutralization capacity for presently available SARS-Cov-2 vaccines. Despite the dampened immune responses documented for some SARS-Cov-2 mutations, available vaccines appear to maintain an overall satisfactory protective activity against most variants of concern (VoC). This may be attributed, at least in part, to cell-mediated immunity. Indeed, the widely multi-specific nature of CD8 T cell responses should allow to avoid VoC-mediated viral escape, because mutational inactivation of a given CD8 T cell epitope is expected to be compensated by the persistent responses directed against unchanged co-existing CD8 epitopes. This is particularly relevant because some immunodominant CD8 T cell epitopes are located within highly conserved SARS-Cov-2 regions that cannot mutate without impairing SARS-Cov-2 functionality. Importantly, some of these conserved epitopes are degenerate, meaning that they are able to associate with different HLA class I molecules and to be simultaneously presented to CD8 T cell populations of different HLA restriction. Based on these concepts, vaccination strategies aimed at potentiating the stimulatory effect on SARS-Cov-2-specific CD8 T cells should greatly enhance the efficacy of immunization against SARS-Cov-2 variants. Our review recollects, discusses and puts into a translational perspective all available experimental data supporting these “hot” concepts, with special emphasis on the structural constraints that limit SARS-CoV-2 S-protein evolution and on potentially invariant and degenerate CD8 epitopes that lend themselves as excellent candidates for the rational development of next-generation, CD8 T-cell response-reinforced, COVID-19 vaccines.

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