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.

Ex Input:
Background: ISG15 is an Ubiquitin-like protein, highly induced by Type I Interferons. Upon the cooperative activity of specific Ubiquitinating enzymes, ISG15 can be conjugated to its substrates. Increasing evidence points to a role for protein ISGylation in anti-viral and anti-tumoral defense. Principal Findings: We identified ISG15 from Old World Monkeys (OWm) as a hyper-efficient protein modifier. Western blot analysis visualized more efficient conjugation of OWmISG15 relative to HuISG15 in human (Hu), monkey and mouse (Mo) cell-lines. Moreover, the substrates of OWmISG15 identified upon Tandem Affinity Purification followed by LC-MS/MS identification largely outnumbered these of HuISG15 itself. Several Ubiquitin-Conjugating enzymes were identified as novel ISGylated substrates. Introduction of a N89D mutation in HuISG15 improved its ISGylation capacity, and additional Q31K/ T33A/D133N mutations yielded a HuISG15 variant with an ISGylation efficiency comparable to OWmISG15. Homology modeling and structural superposition situate N89 in the interaction interface with the Activating enzyme. Analysis of the UbE1L residues in this interface revealed a striking homology between OWmUbE1L and HuUbE1, the Activating enzyme of Ubiquitin. In line with this observation, we found efficient activation of AgmISG15, but not HuISG15 or MoISG15, by HuUbE1, thus providing a likely explanation for OWm hyperISGylation. Conclusions: This study discloses the poor conjugation competence of HuISG15 compared to OWmISG15 and maps the critical determinants for efficient conjugation. HyperISGylation may greatly assist ISGylation studies and may enhance its function as positive regulator of Interferon-related immune responses or as anti-tumoral modulator.

Ex Output:
HyperISGylation of Old World Monkey ISG15 in Human Cells


Ex Input:
Please cite this article as: El-Shall N.A., Shewita R.S., Abd El-Hack M.E., AlKahtane A., Alarifi S., Alkahtani S., Abdel-Daim M.M. & Sedeik M.E., Effect of essential oils on the immune response to some viral vaccines in broiler chickens, with special reference to Newcastle disease virus, Poultry Science (2020), doi: https://doi.(Mohamed E. Abd El-Hack). 21 (1952±28.82) did not significantly (p>0.05) improve growth performance compared to 41 the non-treated birds (NC and VC) (1970±19.56 and 1904±38.66). Essential oils 42 showed an antiviral effect on vNDv in vivo (in chickens) as a preventive measure 43 (PRV) as well as some therapeutic effect (TTT) through decreasing the viral shedding 44 titres (loNC 0 ), mortality rate, and severity of clinical signs and post mortem lesions, in 45 addition to serum malondialdhyde (MDA) level. Regarding the other viruses, the EOs 46 mixture did not improve the immune response to the AI and IB vaccines but age (2108±341.05). The studied EOs mixture showed an immune stimulating response 49 to ND and IBD vaccines, antiviral effect against ND virus especially if administered 50 before the challenge, however it did not have a growth promoting effect. 51 52

Ex Output:
Journal Pre-proof Effect of essential oils on the immune response to some viral vaccines in broiler chickens, with special reference to Newcastle disease virus Effect of essential oils on the immune response to some viral vaccines in broiler 3 chickens, with special reference to Newcastle disease virus 4


Ex Input:
We have investigated the role of two polymorphic sites (R190W and N192K) on the binding and activation of the formyl peptide receptor (FPR) by viral and formyl peptides. WEDWVGWI, a peptide with antiviral activity derived from the membrane proximal region of feline immunodeficiency virus, binds with high affinity to FPR. The three tryptophans in the peptide are all essential for FPR binding, just as they were essential for antiviral activity [S. Giannecchini, A. Di Fenza, A.M. D'Ursi, D. Matteucci, P. Rovero, M. Bendinelli, Antiviral activity and conformational features of an octapeptide derived from the membrane-proximal ectodomain of the feline immunodeficiency virus transmembrane glycoprotein, J. Virol. 77 (2003) 3724]. Formyl-NleWEDWVGWI behaved as a weak partial agonist with FPR W190/N192 but a stronger partial agonist with FPR R190/K192 and FPR R190/N192. Formyl-NleNleWEDWVGWI behaved as a full agonist toward all three FPRs but exhibited a much higher EC 50 with W190/N192 FPR (300 ± 45 nM) than for R190/K192 FPR (40 ± 3 nM) or R190/N192 (60 ± 8 nM). Formyl-MYKWPWYVWL preferentially activated R190/K192 and R190/N192 FPRs by N 5 fold compared to W190/N192 FPR. Formyl-MFEDAVAWF, a peptide derived from a protein in Mycobacterium avium subsp. paratuberculosis and formyl-MFTFEPFPTN, a peptide derived from the N-terminus of chemotaxis inhibitory protein of Staphylococcus aureus with an added N-terminal formyl-methionine exhibited the greatest selectivity for R190/K192 and R190/N192 FPRs with ∼10 fold lower EC 50 s than that observed with FPR W190/N192. Thus, individuals with the W190 polymorphism may display a reduced ability to detect certain formyl peptides.

Ex Output:

Differential activation of polymorphisms of the formyl peptide receptor by formyl peptides