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: The role of CC chemokine ligand 3 (CCL3) in activation of dendritic cells (DCs) following mouse hepatitis virus (MHV) infection of the central nervous system (CNS) was examined. The results indicate that CCL3 participates in an effective host response to MHV infection by contributing to CD11c + CD11b + CD8a À DC maturation, activation, and migration to cervical lymph nodes (CLN). Diminished CD8a À DC activation correlated with reduced IFN-g expression by virus-specific T cells accompanied by increased IL-10 production suggesting that CCL3 contributes to an effective host response to viral infection by enhancing the T cell activation potential of DC. D 
 Title: The CC chemokine ligand 3 regulates CD11c + CD11b + CD8a À dendritic cell maturation and activation following viral infection of the central nervous system: implications for a role in T cell activation

A: False
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Q: Paragraph: Assembly of virus capsids and surface proteins must be regulated to ensure that the resulting complex is an infectious virion. Here we examine assembly of virus capsids, focusing on hepatitis B virus and bacteriophage MS2, and formation of glycoproteins in the alphaviruses. These systems are structurally and biochemically well-characterized and are simplest-case paradigms of self-assembly. Published data suggest that capsid and glycoprotein assembly is subject to allosteric regulation, that is, regulation at the level of conformational change. The hypothesis that allostery is a common theme in viruses suggests that deregulation of capsid and glycoprotein assembly by small molecule effectors will be an attractive antiviral strategy, as has been demonstrated with hepatitis B virus. 
 Title: Virus assembly, allostery, and antivirals

A: False
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Q: Paragraph: A CTL antigenic site located between residues 273 and 291 of the E1 envelope protein of RV was identified by 51Cr_release assays employing SPs. Two E 1specific CTL clones were examined for immune recognition of RV wild-type and attenuated vaccine strains and recombinant E1 protein. The exact sequence (273-284) recognized by both clones was delineated by using truncated and overlapping SPs covering these residues. The defined T-cell site overlapped almost completely with a virus neutralizing antibody-binding site previously identified with mouse monoclonal and human antibodies. A series of single aa-substituted SP analogues of E1(273-284) was used to define residues critical for T-cell recognition. Using EBV-BL displaying different HLA-DR haplotypes and -DR4 subtypes as targets to determine MHC class II restriction elements, immune recognition by both T-cell clones was shown to be associated with HLA-DR4. Three HLA-DR4 subtypes (DR4Dw13A, DR4Dw13B, and DR4KT2) sharing a common residue, glutamic acid at position 74 in their ~ 1 chains, were able to present SP E1(273-284) to the T-cell clones. 
 Title: Analysis of Overlapping T-and B-Cell Antigenic Sites on Rubella Virus E1 Envelope Protein Influence of HLA-DR4 Polymorphism on T-Cell Clonal Recognition

A:
False
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