9,346 research outputs found
LL-18 binds directly to virus particles.
No full text(A) 1H NMR data showing the chemical shifts. Spectra of LL-37 (left panel) or LL-18 (right panel) peptide in the absence or presence of EV71 virus (green line) or CVB5 virus (red line). (B-C) 293T cells cotransfected with GFP or GFP-tagged LL-18 (B) or LL-37 (C) and HA-tagged VP1, VP2, or VP3 plasmids were immunoprecipitated with anti-HA antibody, and interactions between LL-18 and viral structural proteins were detected by anti-GFP antibody.</p
LL-ELM: A regularized extreme learning machine based on L-1-norm and Liu estimator
No full textWOS:000623741500003In this paper, we proposed a novel regularization and variable selection algorithm called Liu-Lasso extreme learning machine (LL-ELM) in order to deal with the ELM's drawbacks like instability, poor generalizability and underfitting or overfitting due to the selection of inappropriate hidden layer nodes. Liu estimator, which is a statistically biased estimator, is considered in the learning phase of the proposed algorithm with Lasso regression approach. The proposed algorithm is compared with the conventional ELM and its variants including ELM forms based on Liu estimator (Liu-ELM), L-1-norm (Lasso-ELM), L-2-norm (Ridge-ELM) and elastic net (Enet-ELM). Convenient selection methods for the determination of tuning parameters for each algorithm have been used in comparisons. The results show that there always exists a d value such that LL-ELM overperforms either Lasso-ELM or Enet-ELM in terms of learning and generalization performance. This improvement in LL-Lasso over Lasso-ELM and Enet-ELM in the sense of testing root mean square error varies up to 27% depending on the proposed d selection methods. Consequently, LL-ELM can be considered as a competitive algorithm for both regressional and classification tasks because of easy integrability property
LL-18 interferes with virus-SCARB2 interaction.
No full text(A) Molecular docking model of LL-18 with EV71 virion. EV71 capsid proteins VP1 (green), VP2 (pink), and VP3(blue), all interact with LL-18 displayed in red sticks (left panel). The amino acid residues of capsid protein interacting with both LL-18 and SCARB2 are indicated (right panel). (B) 293T cells expressing SCARB2-Flag were lysed and cell lysates were incubated with EV71 virus in the absence or presence of the indicated amount of LL-18. Cell lysates were then immunoprecipitated with anti-Flag antibody and the precipitated virus was determined with anti-VP1 antibody. (C) 293T cells expressing Annexin 2-Flag were lysed and cell lysates were incubated with EV71 virus in the absence or presence of LL-18. Cell lysates were then immunoprecipitated with anti-Flag antibody and the precipitated virus was determined with anti-VP1 antibody.</p
LL-18 inhibits mEV71 infection <i>in vivo</i>.
No full text(A) mEV71 was pre-treated with PBS or LL-18 and used to infect 6-day old ICR mice. The survival rate of mice infected with the mEV71 virus with or without LL-18 was recorded. (B) Mice infected with the mEV71 virus with or without LL-18 pre-treatment were sacrificed 1 day post infection (d.p.i.) and viral titers from brain and muscle tissues were determined. ***, P<0.001. (C) H&E staining of muscle tissue from mice infected with the mEV71 virus with or without LL-18. Blue arrows indicate infiltrated neutrophils. Bar, 20μm.</p
LL-18 binds directly to virus particles.
No full text(A) RD cells were pre-incubated with indicated amounts of LL-18, FF-18, DL-37, or LL-37 for 2 hrs before they were washed extensively to remove unbound peptides. Cells were then infected with the EV71 virus (MOI = 1) and cell viability was determined 24 h.p.i. Values were normalized to uninfected RD cells. ***, P1H NMR spectra of FF-18 peptide in the absence or presence of EV71 virus (green line) or CVB5 virus (red line). (TIF)</p
LL-18 did not induce virus resistance.
No full text(A) Diagram of resistance induction assay. (B) RD cells infected with parental EV71 or P30 with or without 1.5 μM LL-18 pre-incubation were tested for cell viability 24 h.p.i. ns, not significant; ***, P<0.001.</p
Significance of LL-37 on Immunomodulation and Disease Outcome
No full textLL-37, also called cathelicidin, is an important part of the human immune system, which can resist various pathogens. A plethora of experiments have demonstrated that it has the multifunctional effects of immune regulation, in addition to antimicrobial activity. Recently, there have been increasing interest in its immune function. It was found that LL-37 can have two distinct functions in different tissues and different microenvironments. Thus, it is necessary to investigate LL-37 immune functions from the two sides of the same coin. On the one side, LL-37 promotes inflammation and immune response and exerts its anti-infective and antitumor effects; on the other side, it has the ability to inhibit inflammation and promote carcinogenesis. This review presents a brief summary of its expression, structure, and immunomodulatory effects as well as brief discussions on the role of this small peptide as a key factor in the development and treatment of various inflammation-related diseases and cancers.Full Tex
LL-18 and FF-18 effectively inhibit EV71 infection.
No full text(A-D) Cell viability of RD cells treated with the indicated amount of DL-37 (A), LL-37 (B), LL-18 (C), or FF-18 (D) was plotted against peptide concentration, and the cytotoxicity was determined. (E) EV71 virus pre-incubated with indicated amounts of DL-37, and the cell viability was determined 24 h.p.i. ***, P (TIF)</p
LL-18 stabilizes the viral particles by inhibiting uncoating.
No full text(A) EV71 virus (MOI = 10) was pre-incubated with PBS, indicated amount of LL-18 or NaCl for 1 hr and then mixed with SYBR green dyes II before they were heated to indicated temperatures. The fluorescent signals were measured and plotted against temperature. PBS was used as a negative control. (B) EV71 virus (MOI = 10) was pre-incubated with PBS, LL-18, or 12s for 2 hrs. Half of the samples were then treated with 1.5 μg SCARB2 protein and incubated at 37°C for 2 hrs at pH 5.5. Samples were then subjected to ultracentrifugation as detailed in materials and methods. The numbers above represent the fractions collected from top to bottom.</p
LL-18 and FF-18 inhibit viral attachment and internalization.
No full text(A) EV71 virus (MOI = 10) was pre-incubated with 3 μM LL-18 or FF-18 before they were used to incubate with RD cells at 4°C for 1 hr. Cells were then washed extensively and kept cultured for 24 hrs before viral VP1 expression was determined with immunoblotting. (B) EV71 virus (MOI = 10) was pre-incubated with 3 μM LL-18 or FF-18 before they were used to incubate with RD cells at 4°C for 1 hr followed by 37°C incubation for 1 hr. Cells were then washed extensively and kept cultured for 24 hrs before viral VP1 expression was determined with immunoblotting. (TIF)</p
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