In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

[Q]: We evaluated the safety and immunogenicity of a chimeric alphavirus vaccine candidate in mice with selective immunodeficiencies. This vaccine candidate was highly attenuated in mice with deficiencies in the B and T cell compartments, as well as in mice with deficient gamma-interferon responsiveness. However, the level of protection varied among the strains tested. Wild type mice were protected against lethal VEEV challenge. In contrast, alpha/beta (αβ) TCR-deficient mice developed lethal encephalitis following VEEV challenge, while mice deficient in gamma/delta ( γδ) T cells were protected. Surprisingly, the vaccine potency was diminished by 50% in animals lacking interferon-gamma receptor alpha chain (R1)-chain and a minority of vaccinated immunoglobulin heavy chain-deficient (μMT) mice survived challenge, which suggests that neutralizing antibody may not be absolutely required for protection. Prolonged replication of encephalitic VEEV in the brain of pre-immunized mice is not lethal and adoptive transfer experiments indicate that CD3 + T cells are required for protection.
[A]: Alpha-beta T cells provide protection against lethal encephalitis in the murine model of VEEV infection


[Q]: Among RNA viruses, the order Nidovirales stands out for including viruses with the largest RNA genomes currently known. Nidoviruses employ a complex RNAsynthesizing machinery comprising a variety of non-structural proteins (nsps). One of the postulated drivers of the expansion of nidovirus genomes is the presence of a proofreading 3 -to-5 exoribonuclease (ExoN) belonging to the DEDDh family. ExoN may enhance the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. Here, we review our current understanding of ExoN evolution, structure, and function. Most experimental data are derived from studies of the ExoN domain of coronaviruses (CoVs), which were triggered by the bioinformatics-based identification of ExoN in the genome of severe acute respiratory syndrome coronavirus (SARS-CoV) and its relatives in 2003. Although convincing data supporting the proofreading hypothesis have been obtained, from biochemical assays and studies with CoV mutants lacking ExoN functionality, the features of ExoN from most other nidovirus families remain to be characterized. Remarkably, viable ExoN knockout mutants were obtained only for two CoVs, mouse hepatitis virus (MHV) and SARS-CoV, whose RNA synthesis and replication kinetics were mildly affected by the lack of ExoN function. In several other CoV species, ExoN inactivation was not tolerated, and knockout mutants could not be rescued when launched using a reverse genetics system. This suggests that ExoN is also critical for primary viral RNA synthesis, a property that poorly matches the profile of an enzyme that would merely boost longterm replication fidelity. In CoVs, ExoN resides in a bifunctional replicase subunit (nsp14) whose C-terminal part has (N7-guanine)-methyltransferase activity. The crystal structure of SARS-CoV nsp14 has shed light on the interplay between these two domains, and on nsp14's interactions with nsp10, a co-factor that strongly enhances ExoN activity in vitro assays. Further elucidation of the structure-function relationships of ExoN and its interactions with other (viral and/or host) members of the CoV replication machinery will be key to understanding the enzyme's role in viral RNA synthesis and pathogenesis, and may contribute to the design of new approaches to combat emerging nidoviruses.
[A]: The Curious Case of the Nidovirus Exoribonuclease: Its Role in RNA Synthesis and Replication Fidelity


[Q]: The viral cytotoxic T lymphocyte (CTL) epitope peptides presented by classical MHC-I 13 molecules require the assembly of a peptide-MHC-I-β2m (aka pMHC-I) trimolecular complex 14 for TCR recognition, which is the critical activation link for triggering antiviral T cell immunity. 15 Ursidae includes 5 genera and 8 species; however, research on T cell immunology in this family, 16 especially structural immunology, is lacking. In this study, the structure of the key trimolecular 17 complex pMHC-1 (aka pAime-128), which binds a peptide from canine distemper virus, was solved 18 for the first time using giant panda as a representative species of Ursidae. The structural 19 characteristics of the giant panda pMHC-I complex, including the unique pockets in the 20 peptide-binding groove (PBG), were analyzed in detail. Comparing the panda pMHC-I to others 21 in the bear family and extending the comparison to other mammals revealed distinct features. 22 Spriggs H, Dear PH, Briggs AW. 2008. Mitochondrial genomes reveal an explosive radiation 469 of extinct and extant bears near the Miocene-Pliocene boundary. Bmc Evolutionary Biology 470 8:220-220. 471 22. et al. 2009. The sequence and de novo assembly of the 476 giant panda genome. Nature 463:311. 477 Pan HJ, Wan QH, Fang SG. 2008. Molecular characterization of major histocompatibility 478 complex class I genes from the giant panda (Ailuropoda melanoleuca). Immunogenetics
[A]:
Crystal structure of the giant panda MHC class I complex: first insights into the viral 1 peptide presentation profile in the bear family 2