In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

Q: Objective: Health literacy has become a global issue, and it is important that patients and individuals are able to use information technology to access health information and educational services. The research objective is to develop a Saudi e-health literacy scale (SeHL) for measuring e-health literacy among Saudis suffering from non-communicable diseases (NCD). Methods: Overall, 14 relevant papers in related interdisciplinary fields were reviewed to select the most useful literacy dimensions. From these articles, we extracted the most common dimensions used to measure e-health literacy across the disciplines. Multiple workshops with multidisciplinary team members reviewed and evaluated items for SeHL. Results: Four key aspects of e-health literacy-use of technology/media, information-seeking, usefulness and confidence-were identified and integrated as e-health literacy dimensions. These will be used to measure e-health literacy among Saudi patients with NCDs. A translation from Arabic to English was performed in order to ensure that translation process was accurate. A SeHL scale was developed to measure e-health literacy among Saudi patients. By understanding e-health literacy levels, we will be able to create a patient-education system to be used by patients in Saudi Arabia. Conclusions: As information technology is increasingly used by people of all ages all over the world, e-health literacy has been identified as a key factor in determining health outcomes. To date, no comprehensive scale exists to assess e-health literacy levels among speakers of Arabic, particularly among people with NCD such as diabetes, cardiovascular diseases and hypertension.

A: Saudi Arabia, 5 Prince Sultan Military Medical City, AlSulimaniah, Riyadh 11159, Saudi Arabia, 6 King Faisal Specialist and Research Center
****
Q: We determined the interferon- (IFN-) cDNA sequence from three porcine breeds, Duroc, Landrance/Duroc hybrid, and Landrance breeds. Five single nucleotide polymorphisms (SNPs) of porcine IFN- (PoIFN-) were identified, respectively, at positions 269 (A/G), 376 (C/T), 426 (T/C), and 465 (T/C) of the coding sequence in Landrance/Duroc hybrid, and at position 251 (A/G) in Landrance breed. Among them, A269G and A251G polymorphisms resulted in Q67R and K61R replacements in the mature protein. PoIFN- cDNAs of Duroc breed (PoIFN--W) and Landrance/Duroc hybrid (PoIFN--M), which, respectively, encoded Q67 and R67, were introduced into a prokaryotic expression vector pET32 to express recombinant PoIFN--W (rPoIFN--W) and rPoIFN--M protein variants in Escherichia coli. The identity of both protein variants was further confirmed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). We then compared bioactivities of these two recombinant proteins. Although both recombinant protein variants exhibited comparable activities in antiproliferation of PK-15 cells and in nitric oxide (NO) induction of porcine peripheral monocytes, antiviral activity of rPoIFN--W protein was significantly higher (P < 0.001) than that of rPoIFN--M protein in a plaque inhibition assay using pseudorabies virus (PRV). IC50 values of rPoIFN--W and rPoIFN--M protein in anti-PRV assay were determined as 5.3 1.3 and 9.3 4.3 nM, respectively. In conclusion, we have identified five novel SNPs in PoIFN- cDNA, including two missense polymorphisms that result in Q67R and K61R replacements. Our results further demonstrate that Q67R can markedly reduce antiviral activity of the PoIFN- protein. This is the first report that shows the functional SNP in the coding region of IFN-. In the future, it is imperative to determine whether Q67R replacement in IFN- may have disease association.

A: A missense polymorphism in porcine interferon- cDNA affects antiviral activity of the protein variant
****
Q: The tripartite motif (TRIM)-containing proteins usually exert important regulatory roles during multiple biological processes. TRIM8 has been demonstrated to be a RING domain-containing E3 ubiquitin ligase which plays critical roles in inflammation and cancer. In this study, a TRIM8 homolog from grouper, Epinephelus coioides (EcTRIM8) was cloned, and its effects on fish virus replication were investigated. The full-length EcTRIM8 cDNA encoded a polypeptide of 568 amino acids with 92% identity to TRIM8 homolog from large yellow croaker (Larimichthys crocea). Sequence alignment analysis indicated that EcTRIM8 contained conserved RING finger, B-box and coiled-coil domain. Expression patterns analysis showed that EcTRIM8 was predominant in kidney, gill, fin, liver, spleen and brain. After challenging with Singapore grouper iridovirus (SGIV) or polyinosin-polycytidylic acid (poly I:C), the EcTRIM8 transcript was significantly increased at the early stage of injection. Under fluorescence microscopy, we observed different distribution patterns of EcTRIM8 in grouper spleen (GS) cells, including punctate fluorescence evenly situated throughout the cytoplasm and bright aggregates. The ectopic expression of EcTRIM8 in vitro significantly inhibited the replication of SGIV and red spotted grouper nervous necrosis virus (RGNNV), evidenced by the obvious reduction in the severity of cytopathic effect (CPE) and the significant decrease in viral gene transcription and protein synthesis. Moreover, the transcription of the proinflammatory factors and interferon related immune factors were differently regulated by EcTRIM8 during SGIV or RGNNV infection. In addition, overexpression of EcTRIM8 significantly increased the transcription of interferon regulator factor 3 (IRF3) and IRF7, and enhanced IRF3 or IRF7 induced interferon-stimulated response element (ISRE) promoter activity. Together, our results firstly demonstrated that fish TRIM8 could exert antiviral function through the regulation of the expression of proinflammatory cytokines and interferon related transcription factors in response to fish viruses.

A:
Fish TRIM8 exerts antiviral roles through regulation of the proinflammatory factors and interferon signaling
****