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".

[Q]: Paragraph: Hepatitis C Virus (HCV) infects 2% of the world's population and is the leading cause of liver disease and liver transplantation. It poses a serious and growing worldwide public health problem that will only be partially addressed with the introduction of new antiviral therapies. However, these treatments will not prevent re-infection particularly in high risk populations. The introduction of a HCV vaccine has been predicted, using simulation models in a high risk population, to have a significant effect on reducing the incidence of HCV. A vaccine with 50 to 80% efficacy targeted to high-risk intravenous drug users could dramatically reduce HCV incidence in this population. Virus like particles (VLPs) are composed of viral structural proteins which self-assemble into non-infectious particles that lack genetic material and resemble native viruses. Thus, VLPs represent a safe and highly immunogenic vaccine delivery platform able to induce potent adaptive immune responses. Currently, many VLP-based vaccines have entered clinical trials, while licensed VLP vaccines for hepatitis B virus (HBV) and human papilloma virus (HPV) have been in use for many years. The HCV core, E1 and E2 proteins can self-assemble into immunogenic VLPs while inclusion of HCV antigens into heterogenous (chimeric) VLPs is also a promising approach. These VLPs are produced using different expression systems such as bacterial, yeast, mammalian, plant, or insect cells. Here, this paper will review HCV VLP-based vaccines and their immunogenicity in animal models as well as the different expression systems used in their production. 
 Title: Preclinical Development and Production of Virus-Like Particles As Vaccine Candidates for Hepatitis C
[A]: True


[Q]: Paragraph: The infection of the avian coronavirus infectious bronchitis virus (IBV) is initiated by the binding of the spike glycoprotein S to sialic acids on the chicken host cell. In this study we identified the receptorbinding domain (RBD) of the spike of the prototype IBV strain M41. By analyzing the ability of recombinantly expressed chimeric and truncated spike proteins to bind to chicken tissues, we demonstrate that the N-terminal 253 amino acids of the spike are both required and sufficient for binding to chicken respiratory tract in an α-2,3-sialic acid-dependent manner. Critical amino acids for attachment of M41 spike are present within the N-terminal residues 19-69, which overlap with a hypervariable region in the S1 gene. Our results may help to understand the differences between IBV S1 genotypes and the ultimate pathogenesis of IBV in chickens. 
 Title: Mapping of the receptor-binding domain and amino acids critical for attachment in the spike protein of avian coronavirus infectious bronchitis virus
[A]: True


[Q]: Paragraph: New possibilities for the design of coronavirus vaccines have been opened up with the elucidation of the structure of the receptorbinding domain (RBD) of severe acute respiratory syndrome (SARS) spike protein. The RBD of the SARS spike protein is responsible for virus attachment to its receptor, angiotensinconverting enzyme-2 (ACE2), on human cells. The RBD of the human epidemic strain differs from that of the animal virus by just two amino acids. Harrison and colleagues determined the complex of the interacting segments of these proteins, which consists of residues 19-615 of the peptidase domain of human ACE2 and residues 323-502 of the RBD, to 2.9-Å resolution. The ACE2 peptidase domain comprises two lobes that close during substrate binding, and the spike RBD contacts the tip of one lobe when ACE2 is either open or closed. The RBD has a five-stranded, antiparallel β-sheet core, and an extended-loop subdomain that lies along one edge of the core. A two-stranded β-sheet in this loop forms a concave surface that cradles the N-terminal helix of ACE2, and ridges along either side of the loop interact with structural features of ACE2. This loop (residues 424-494) was named the receptor-binding motif (RBM) and makes the only contacts with ACE2, producing a 1,700 Å 2 interface that is consistent with the high binding affinity of these proteins (K d ~10 -8 ). The detailed analysis of the contacts between these two proteins provides useful information for rational vaccine design. REFERENCE Li, F. et al. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. 
 Title: STRUCTURE WATCH Spikes point the way
[A]:

Show your work and conclude with the exact phrasing "Therefore, the final answer is [answer]." where [answer] is just the final number or expression that solves the problem.
user
False


