instruction:
In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".
question:
Paragraph: A number of emerging and re-emerging viruses have caused epidemics or pandemics of infectious diseases leading to major devastations throughout human history. Therefore, developing effective and safe vaccines against these viruses is clearly important for the protection of at-risk populations. Our previous studies have shown that the receptor-binding domain (RBD) in the spike protein of severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) is a key target for the development of SARS vaccines. In this review, we highlight some key advances in the development of antiviral vaccines targeting the RBDs of spike proteins of emerging and re-emerging viruses, using SARS-CoV, influenza virus, Hendra virus (HeV) and Nipah virus (NiV) as examples. Figure 1 The interaction between the receptor-binding domain in the spike of an emerging virus and the corresponding receptor on the target cell. 
 Title: Emerging Microbes and Infections (2012) 1, e13
answer:
True


question:
Paragraph: Fusion of MHV-3-immune splenocytes from MHV-3-resistant A/J murine strain, with NS myeloma cells produced several hybridomas. Among eight hybridoma clones, the 1E7A4H1 clone secreted kappa IgG2a apparently directed against the nucleoprotein of the MHV-3 virion. The monoclonal antibody was able to neutralize tile in vitro cytopathic effect of MHV-3 on cultured L2 cells, and was detected by indirect immunofluorescence on MHV-3-infected cultured Y AC cells. In addition, it conferred a significant protection against MHV-3-induced acute disease, if injected intraperitoneally to C57BL/6 mice before inoculation with MHV-3. , Mouse hepatitis viruses (MHVs), members of the coronavirus family, produce various diseases i n t h e mouse and other animal species [16] . They exhibit different tissue tropisms and patterns of infection [1]. The susceptibility of the animals to the virus-induced diseases appears to be genetically controlled at different levels [16] . Serological neutralization patterns of several of the MHVs are very complex [11, 15] and the three structural proteins demonstrated variable degrees of conservation [4, 13] . Coronaviruses are frequently endemic in laboratory mouse colonies [8] . Neutralizing monoclonal antibodies have been recently prepared against the J H M (MHV-4) [2, 4, 17] and MHV-2 [9] strains. In this brief note, we report on a monoclonaI antibody, apparently specific for the nueleo-* Present address: Instituto Butantan, Laboratoria Especial de Immunologia Viral, S~o Paulo, Brazil. 
 Title: Archives of Virology Protection from mouse hepatitis virus type 3-induced acute disease by an anti-nucleoprotein monoclonal antibody Brief Report
answer:
True


question:
Paragraph: A combination of comparative sequence analysis and thermodynamic methods reveals the conservation of tertiary structure elements in the 5' untranslated region (UTR) of human enteroviruses and rhinoviruses. The predicted common structural elements occur in the 3' end of a segment that is critical for internal ribosome binding, termed "ribosome landing pad" (RLP), of polioviruses. Base pairings between highly conserved 17-nucleotide (nt) and 21 -nt sequences in the 5' UTR of human enteroviruses and rhinoviruses constitute a predicted pseudoknot that is significantly more stable than those that can be formed from a large set of randomly shuffled sequences. A conserved singlestranded polypyrimidine tract is located between two conserved tertiary elements. R. Nicholson, J. Pelletier, S.-Y. Le, and N. Sonenberg (1991, J. l&o/. 65, 5886-5894) demonstrated that the point mutations of 3-nt UUU out of an essential 4-nt pyrimidine stretch sequence UUUC abolished translation. Structural analysis of the mutant sequence indicates that small point mutations within the short polypyrimidine sequence would destroy the tertiary interaction in the predicted, highly ordered structure. The proposed common tertiary structure can offer experimentalists a model upon which to extend the interpretations for currently available data. Based on these structural features possible base-pairing models between human enteroviruses and 18 S rRNA and between human rhinoviruses and 18 S rRNA are proposed. The proposed common structure implicates a biological function for these sequences in translational initiation. 
 Title: Conserved Tertiary Structure Elements in the 5' Untranslated Region of Human Enteroviruses and Rhinoviruses
answer:

False