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".

Ex Input:
Paragraph: Purpose: Receiving influenza vaccination may increase the risk of other respiratory viruses, a phenomenon known as virus interference. Test-negative study designs are often utilized to calculate influenza vaccine effectiveness. The virus interference phenomenon goes against the basic assumption of the test-negative vaccine effectiveness study that vaccination does not change the risk of infection with other respiratory illness, thus potentially biasing vaccine effectiveness results in the positive direction. This study aimed to investigate virus interference by comparing respiratory virus status among Department of Defense personnel based on their influenza vaccination status. Furthermore, individual respiratory viruses and their association with influenza vaccination were examined. Results: We compared vaccination status of 2880 people with non-influenza respiratory viruses to 3240 people with pan-negative results. Comparing vaccinated to non-vaccinated patients, the adjusted odds ratio for non-flu viruses was 0.97 (95% confidence interval (CI): 0.86, 1.09; p = 0.60). Additionally, the vaccination status of 3349 cases of influenza were compared to three different control groups: all controls (N = 6120), non-influenza positive controls (N = 2880), and pan-negative controls (N = 3240). The adjusted ORs for the comparisons among the three control groups did not vary much (range: 0.46-0.51). Conclusions: Receipt of influenza vaccination was not associated with virus interference among our population. Examining virus interference by specific respiratory viruses showed mixed results. Vaccine derived virus interference was significantly associated with coronavirus and human metapneumovirus; however, significant protection with vaccination was associated not only with most influenza viruses, but also parainfluenza, RSV, and non-influenza virus coinfections. Published by Elsevier Ltd.
Title: Influenza vaccination and respiratory virus interference among Department of Defense personnel during the 2017-2018 influenza season

Ex Output:
False

Ex Input:
Paragraph: Tilapia lake virus (TiLV) is a negative-sense single-stranded RNA (-ssRNA) icosahedral virus classified to be the only member in the family Amnoonviridae. Although TiLV segment-1 shares homology with the influenza C virus PB1 and has four conserved motifs similar to influenza A, B, and C polymerases, it is unknown whether there are other properties shared between TiLV and orthomyxovirus. In the present study, we wanted to determine whether TiLV agglutinated avian and piscine erythrocytes, and whether its replication was inhibited by lysosomotropic agents, such as ammonium chloride (NH 4 Cl), as seen for orthomyxoviruses. Our findings showed that influenza virus strain A/Puerto Rico/8 (PR8) was able to hemagglutinate turkey (Meleagris gallopavo), Atlantic salmon (Salmo salar L), and Nile tilapia (Oreochromis niloticus) red blood cells (RBCs), while infectious salmon anemia virus (ISAV) only agglutinated Atlantic salmon, but not turkey or tilapia, RBCs. In contrast to PR8 and ISAV, TiLV did not agglutinate turkey, Atlantic salmon, or tilapia RBCs. qRT-PCR analysis showed that 30 mM NH 4 Cl, a basic lysosomotropic agent, neither inhibited nor enhanced TiLV replication in E-11 cells. There was no difference in viral quantities in the infected cells with or without NH 4 Cl treatment during virus adsorption or at 1, 2, and 3 h post-infection. Given that hemagglutinin proteins that bind RBCs also serve as ligands that bind host cells during virus entry leading to endocytosis in orthomyxoviruses, the data presented here suggest that TiLV may use mechanisms that are different from orthomyxoviruses for entry and replication in host cells. Therefore, future studies should seek to elucidate the mechanisms used by TiLV for entry into host cells and to determine its mode of replication in infected cells.
Title: Tilapia Lake Virus Does Not Hemagglutinate Avian and Piscine Erythrocytes and NH 4 Cl Does Not Inhibit Viral Replication In Vitro

Ex Output:
True

Ex Input:
Paragraph: that can be specifically targeted by fusion-inhibitory peptides. Antiviral potency can be improved by sequence modification and lipid conjugation, and by adding linkers between the protein and lipid components. We exploit the uniquely broad spectrum antiviral activity of a parainfluenza F-derived peptide sequence that inhibits both parainfluenza and Nipah viruses, to investigate the influence of peptide orientation and intervening linker length on the peptides' interaction with transitional states of F, solubility, membrane insertion kinetics, and protease sensitivity. We assessed the impact of these features on biodistribution and antiviral efficacy in vitro and in vivo. The engineering approach based on biophysical parameters resulted in a peptide that is a highly effective inhibitor of both paramyxoviruses and a set of criteria to be used for engineering broad spectrum antivirals for emerging paramyxoviruses. Human parainfluenza viruses (HPIVs) are paramyxoviruses belonging to the respirovirus (HPIV1 and 3) or rubulavirus (HPIV2 and 4) genera that cause human respiratory diseases including bronchitis, bronchiolitis, and pneumonia in infants, children, or immune-compromised individuals. The HPIV species viruses are responsible for 30-40% of all acute respiratory tract infections in infants and children 1 . Nipah virus (NiV) is a zoonotic paramyxovirus of the henipavirus genus that represents a global health risk with broad, unpredictable pandemic potential. Infection with this virus is devastating, rapidly causing a generalized vasculitis leading to lethal encephalitis and serious respiratory infections. The common natural reservoirs of henipavirus genus members (including NiV, Hendra virus, Cedar virus and numerous newly identified species) are fruit bats 2,3 , but recent identification of rodent-origin henipa-like viruses that cause lethal respiratory disease in humans suggests that the range of natural mammalian hosts may be even broader 4 . Transmitted by air or food, its mechanism of infection is complex, and no drugs exist to prevent or treat infection. The recent human-to-human spread of NiV in Asia has raised the real possibility of global spread. NiV and HPIV, while different in their associated diseases and geography, infect using similar mechanisms and are vulnerable to the same antiviral strategy. Paramyxovirus infections are initiated by fusion between viral and host cell membranes. For HPIV3, NiV, and other paramyxoviruses, the surface glycoproteins play critical roles in the initial events of viral infection, mediating virion attachment to cells and fusion of the viral and cellular membranes. The viral fusion protein (F), upon insertion of the fusion peptide -formed after cleavage of the precursor F into its final fragment -into the host target cell membrane, forms a transient intermediate to pull the viral and cell membranes together. Two heptad-repeat regions that are present in each ectodomain of F refold to form a highly stable, antiparallel six-helix bundle structure that is coupled to membrane fusion. The structure required for this step can be specifically targeted by fusion-inhibitory peptides. The N-terminal repeat (HRN) is adjacent to the hydrophobic fusion peptide that inserts into the target cell membrane during the fusion process. The C-terminal repeat (HRC) immediately precedes the transmembrane domain. A folding-back of the F ectodomain drives the viral membrane towards the cell-associated fusion peptide to bring the two membranes into proximity, causing membrane fusion and viral entry. Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion 5 . We have shown the potential of modified fusion inhibitor peptides as NiV and HPIV antiviral agents, and showed that a sequence corresponding to the HRC domain of HPIV3 effectively inhibits both HPIV3 and NiV 6 . Interhelical packing interactions in the post-fusion core of the NiV and HPIV3 F proteins are important determinants of viral entry and its inhibition. Fusion inhibitor peptides can be engineered at the level of these parameters, for optimal inhibition, increasing potency for both viruses [6] [7] [8] [9] [10] . Conjugating cholesterol to a fusion inhibitor peptide enhances NiV antiviral activity up to 100-fold, by targeting the peptide to the plasma membrane where fusion occurs 8 and endows the fusion inhibitor with the ability to localize to the central nervous system, successfully preventing and treating NiV infection in a golden hamster model of disease 6 . Surprisingly, the most effective antiviral peptides for NiV and the related Hendra virus (HeV) are those derived from the F of HPIV3. The antiviral strategy discussed here exploits the uniquely broad spectrum antiviral activity of these HPIV3 derived inhibitory peptides to treat paramyxovirus infection. In an effort to understand the biophysical properties that correlate with peptide efficacy and thereby improve upon their antiviral utility, we explored biophysical features of the lipid-conjugated peptides that alter aggregation and membrane insertion kinetics. We have identified several properties that correlate with the peptides' potency and permit enhancement of antiviral effect for both HPIV3 and NiV.
Title: Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides Human paramyxoviruses include global causes of lower respiratory disease like the OPEN

Ex Output:
True