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: Background: Household studies provide opportunities to understand influenza-like-illness (ILI) transmission, but data from (sub)tropical developing countries are scarce. Objective: To determine the viral etiology and epidemiology of ILI in households. Study design: ILI was detected by active case finding amongst a cohort of 263 northern Vietnam households between 2008 and 2013. Health workers collected nose and throat swabs for virus detection by multiplex real-time RT-PCR. Results: ILI was detected at least once in 219 (23.7%) of 945 household members. 271 (62.3%) of 435 nose/throat swabs were positive for at least one of the 15 viruses tested. Six viruses predominated amongst positive swabs: Rhinovirus (28%), Influenza virus (17%), Coronavirus (8%), Enterovirus (5%), Respiratory syncytial virus (3%), Metapneumovirus virus (2.5%) and Parainfluenza virus 3 (1.8%). There was no clear seasonality, but 78% of episodes occurred in Winter/Spring for Influenza compared to 32% for Rhinovirus. Participants, on average, suffered 0.49 ILI, and 0.29 virus-positive ILI episodes, with no significant effects of gender, age, or household size. In contrast to US and Australian community studies, the frequency of ILI decreased as the number of household members aged below 5 years increased (p = 0.006). Conclusion: The findings indicate the need for tailored ILI control strategies, and for better understanding of how local childcare practices and seasonality may influence transmission and the role of children.
Title: Epidemiology and etiology of influenza-like-illness in households in Vietnam; it's not all about the kids!
[A]: True

[Q]: Paragraph: Despite the wide use of Caenorhabditis elegans as a model organism, the first virus naturally infecting this organism was not discovered until six years ago. The Orsay virus and its related nematode viruses have a positive-sense RNA genome, encoding three proteins: CP, RdRP, and a novel protein that shares no homology with any other proteins. can be expressed either as a free or a CP- fusion protein by ribosomal frameshift, but the structure and function of both and CP- remain unknown. Using a combination of electron microscopy, X-ray crystallography, computational and biophysical analyses, here we show that the Orsay protein forms a~420-A long, pentameric fiber with an N-terminal -helical bundle, a -stranded filament in the middle, and a C-terminal head domain. The pentameric nature of the fiber has been independently confirmed by both mass spectrometry and analytical ultracentrifugation. Recombinant Orsay capsid containing CP- shows protruding long fibers with globular heads at the distal end. Mutant viruses with disrupted CP- fibers were generated by organism-based reverse genetics. These viruses were found to be either non-viable or with poor infectivity according to phenotypic and qRT-PCR analyses. Furthermore, addition of purified proteins to worm culture greatly reduced Orsay infectivity in a sequence-specific manner. Based on the structure resemblance between the Orsay CP- fiber and the fibers from reovirus and adenovirus, we propose that CP- functions as a cell attachment protein to mediate Orsay entry into worm intestine cells. Orsay, the only virus known to naturally infect the nematode Caenorhabditis elegans, expresses a capsid- fusion protein. We have demonstrated that the Orsay fusion protein is incorporated into Orsay capsid and forms a~420-A long fiber protruding from the PLOS Pathogens |
Title: Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells
[A]: False

[Q]: Paragraph: because of short half-life, drug resistance and cross-reactivity with the preexisting antibodies in HIV-infected patients. Using an artificial peptide strategy, we designed a peptide with non-native protein sequence, AP3, which exhibited potent antiviral activity against a broad spectrum of HIV-1 strains, including those resistant to T20, and had remarkably longer in vivo half-life than T20. While the preexisting antibodies in HIV-infected patients significantly suppressed T20's antiviral activity, these antibodies neither recognized AP3, nor attenuated its anti-HIV-1 activity. Structurally different from T20, AP3 could fold into single-helix and interact with gp41 NHR. The two residues, Met and Thr, at the N-terminus of AP3 form a hook-like structure to stabilize interaction between AP3 and NHR helices. Therefore, AP3 has potential for further development as a new HIV fusion inhibitor with improved antiviral efficacy, resistance profile and pharmacological properties over enfuvirtide. The envelope glycoprotein (Env) of the human immunodeficiency virus type 1 (HIV-1) includes the gp120 surface subunit and the gp41 transmembrane subunit. As a class I transmembrane protein, gp41 plays a significant role in the membrane fusion and virus entry of HIV-1 1,2 . After the binding of the gp120 to the cellular receptors, gp41 undergoes conformation changes after fusion peptide (FP) inserts into the
Title: Improved Pharmacological and Structural Properties of HIV Fusion Inhibitor AP3 over Enfuvirtide: Highlighting Advantages of Artificial Peptide Strategy OPEN
[A]:
True