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: Seven fragments of the spike (S) gene cDNA of transmissible gastroenteritis virus (TGEV), as well as the full length cDNA, were cloned and expressed in baculovirus vectors. Piglets were immunized with cells infected with the recombinant viruses. Each of the recombinants induced TGEV-specific antibodies detected in a fixed cell enzyme immunoassay. The amino terminal half of the S protein, containing all four major antigenic sites (A, B, C and D), and encoded by a 2.2 kb fragment of the S gene, induced virus neutralizing (VN) antibody titers comparable with those induced by the complete S protein. Recombinant proteins lacking the A antigenic site, or with a deletion including the putative receptor binding sites and the D antigenic site, were not capable of inducing levels of VN antibodies similar to those induced by the whole S protein. 
 Title: Immunogenicity of the S protein of transmissible gastroenteritis virus expressed in baculovirus
answer:
False


question:
Paragraph: Rational design of proteins with novel binding specificities and increased affinity is one of the major goals of computational protein design. Epitope-scaffolds are a new class of antigens engineered by transplanting viral epitopes of pre-defined structure to protein scaffolds, or by building protein scaffolds around such epitopes. Epitope-scaffolds are of interest as vaccine components to attempt to elicit neutralizing antibodies targeting the specified epitope. In this study we developed a new computational protocol, MultiGraft Interface, that transplants epitopes but also designs additional scaffold features outside the epitope to enhance antibody-binding specificity and potentially influence the specificity of elicited antibodies. We employed MultiGraft Interface to engineer novel epitope-scaffolds that display the known epitope of HIV-1 neutralizing antibody 2F5 and that also interact with the functionally important CDR H3 antibody loop. MultiGraft Interface generated an epitope-scaffold that bound 2F5 with sub-nanomolar affinity (K D = 400 pM) and that interacted with the antibody CDR H3 loop through computationally designed contacts. Substantial structural modifications were necessary to engineer this antigen, with the 2F5 epitope replacing a helix in the native scaffold and with 15% of the native scaffold sequence being modified in the design stage. This epitope-scaffold represents a successful example of rational protein backbone engineering and protein-protein interface design and could prove useful in the field of HIV vaccine design. MultiGraft Interface can be generally applied to engineer novel binding partners with altered specificity and optimized affinity. § 
 Title: Computational design of protein antigens that interact with the CDR H3 loop of HIV broadly neutralizing antibody 2F5 HHS Public Access
answer:
False


question:
Paragraph: Sanekata, T., Kishimoto, E., Sato, K., Honma, H., Otsuki, K. and Tsubokura, M., 1991. Detection of poricine rotavirus in stools by a latex agglutination test. Vet. Microbiol., 27:245-251. We developed a simple agglutination test for the detection of porcine rotavirus in stools from pigs with diarrhea. The virus was detected with high sensitivity and specificity by a slide agglutination test using latex particles coated with antibody against the porcine rotavirus strain OSU (LA-antiOSU). The agglutination of LA-antiOSU with OSU on a glass slide was evident macroscopically within 2 rain. The sensitivity of this latex agglutination (LA) test was four times higher than that of the electron microscope method. The LA test is available for the rapid diagnosis of porcine rotavirus infections. 
 Title: Detection of porcine rotavirus in stools by a latex agglutination test
answer:

True