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".
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Question: Paragraph: Mice infected with neurotropic strains of coronavirus develop acute encephalomyelitis and eliminate infectious virus. However, control of acute infection is incomplete resulting in persistence of viral RNA in the central nervous system (CNS) associated with ongoing primary demyelination. A high prevalence of virus specific CD8 and CD4 T cells within the CNS correlates with ex vivo cytolytic activity and IFN-7 secretion, which are both required for virus reduction during the acute infection. Although most infected cell types are susceptible to perforin mediated clearance, IFNq' is required for controlling infection of oligodendrocytes. Furthermore, by enhancing class I expression and inducing class II expression within resident CNS cells IFN-7 optimizes T cell receptor dependent functions. In addition to its direct anti viral activity, these multifactorial effects make IFN-y more essential than perforin for viral control. CD4 T cells enhance CD8 T cell expansion, survival and effectiveness. Although both CD8 and CD4 T cells are retained within the CNS during persistence, they cannot control viral recrudescence in the absence of humoral immunity. Demyelination can be mediated by either CD8 or CD4 T cells; however, although a variety of effector molecules have been excluded, a dominant common denominator remains elusive. Thus concerted efforts to control infection coincide with a variety of potential mechanisms causing chronic demyelinating disease. 
 Title: Chapter C4 THE ROLE OF T CELLS IN CORONA-VIRUS- INDUCED DEMYELINATION

Answer: False


Question: Paragraph: In ostriches, the population densities resulting from intensive rearing increases susceptibility to pathogens such as mycoplasmas. In addition to good management practices, vaccination offers an attractive alternative for controlling mycoplasma infections in food animals, instead of using antibiotics, which often leave unacceptable residues. The use of live attenuated vaccines, however, carry the concern of reversion to virulence or genetic recombination with field strains. Currently there are no commercially available vaccines against ostrich-infecting mycoplasmas and this study therefore set out to develop and evaluate the use of a DNA vaccine against mycoplasma infections in ostriches using an OppA protein as antigen. To this end, the oppA gene of "Mycoplasma nasistruthionis sp. nov." str. Ms03 was cloned into two DNA vaccine expression vectors after codon correction by site-directed mutagenesis. Three-months-old ostriches were then vaccinated intramuscularly at different doses followed by a booster vaccination after 6 weeks. The ability of the DNA vaccines to elicit an anti-OppA antibody response was evaluated by ELISA using the recombinant OppA protein of Ms03 as coating antigen. A statistically significant anti-OppA antibody response could be detected after administration of a booster vaccination indicating that the OppA protein was successfully immunogenic. The responses were also both dose and vector dependent. In conclusion, the DNA vaccines were able to elicit an immune response in ostriches and can therefore be viewed as an option for the development of vaccines against mycoplasma infections. 
 Title: DNA Vaccines Against Mycoplasma Elicit Humoral Immune Responses in Ostriches

Answer: False


Question: Paragraph: Background: Lactoferrin (Lf) is an 80 kDa iron-binding glycoprotein of the transferrin family. It is abundant in milk and in most biological fluids and is a cell-secreted molecule that bridges innate and adaptive immune function in mammals. Its protective effects range from anticancer, anti-inflammatory and immune modulator activities to antimicrobial activities against a large number of microorganisms. This wide range of activities is made possible by mechanisms of action involving not only the capacity of Lf to bind iron but also interactions of Lf with molecular and cellular components of both hosts and pathogens. Scope of review: This review summarizes the activities of Lf, its regulation and potential applications. Major conclusions: The extensive uses of Lf in the treatment of various infectious diseases in animals and humans has been the driving force in Lf research however, a lot of work is required to obtain a better understanding of its activity. General significance: The large potential applications of Lf have led scientists to develop this nutraceutical protein for use in feed, food and pharmaceutical applications. This article is part of a Special Issue entitled Molecular Mechanisms of Iron Transport and Disorders. j o u r n a l h o m e p a g e : w w w. e l s ev i e r. c o m / l o c a t e / b b a g e n primates, 7 even-toed ungulates, 1 pig, 1 cat, and 1 mouse. Pairwise sequence identities ranged from a minimum of~78% to nearly 100%. The main outliers in this group were Lfs from primates, in which human and chimpanzee are quite similar (95-98%) when compared to orangutan (79%). On the other hand, horse and camel; pig, cow, yak, water buffalo, bull, and goat Lfs share 81 and 78% of sequence identity respectively when compared to human Lf as outgroup. The sequence relationships given above show that the Lfs form a highly conserved sequence family, and also sequence identity between Lfs and other Tfs is relatively high at 60-65% [19] . A characteristic feature of Lfs is their highly basic character, with a pI typically greater than 9; this property is typically predictable from their sequence. Structurally, the feature that most readily distinguishes Lfs from Tfs is the peptide linker between the two lobes, thought to have evolved from an ancient duplication event [20] , which also contains several proline residues. Lf is an 80 kDa glycosylated protein of~700 amino acids, with a high homology among species. It is comprised of a simple polypeptide chain folded into two symmetrical lobes (the N-lobe and C-lobe), which are highly homologous with one another (33-41% homology). The two lobes are connected via a hinge region containing parts of an α-helix between amino acids 333 and 343 in human Lf (hLf) [7] , which confers flexibility to the molecule [6, 7, 21] . The polypeptide chain includes amino acids 1-332, comprising the N-lobe, and 344-703, comprising the C-lobe, and it is made up of α-helix and β-pleated sheet structures that create two domains within each lobe (domains I and II) [22] . Each lobe can bind a metal atom in synergy with the carbonate ion (CO 3 −2 
 Title: Lactoferrin a multiple bioactive protein: An overview ☆

Answer:
False