NDLI: Identifying the Critical Domain of LL-37 Involved in Mediating Neutrophil Activation in the Presence of Influenza Virus: Functional and Structural Analysis

Content Provider	PubMed Central
Author	Tripathi, Shweta Wang, Guangshun White, Mitchell Rynkiewicz, Michael Seaton, Barbara Hartshorn, Kevan
Editor	Jonas, Waldenström
Copyright Year	2015
Abstract	The human cathelicidin LL-37 has been shown to play a role in host defense against influenza A viruses (IAV) through direct antiviral effects and through modulating inflammatory responses to infection. We recently showed that LL-37 increases neutrophil respiratory burst and neutrophil extracellular trap (NET) responses to IAV through engaging formyl peptide receptor 2 (FPR-2). In this paper we show that a fragment of LL-37, GI-20, which is composed of the central helical segment of the peptide, has similar effects as LL-37 on neutrophil activation. In addition to increasing respiratory burst and NET responses of the cells to IAV through an FPR-2 dependent mechanism, it reduces neutrophil IL-8 production to IAV (also like LL-37). The N-terminal fragment, LL-23, did not have similar effects. Both GI-20 and LL-37 increase neutrophil intracellular calcium levels and their ability to increase neutrophil activation responses was calcium dependent and partially inhibited by pertussis toxin. These studies show that the central helix of LL-37 retains the ability of LL-37 to modulate neutrophil responses through FPR-2. Based on our findings we developed a homology model of FPR-2 and performed docking experiments of LL-37 and GI-20 with the receptor.
Related Links	http://dx.doi.org/10.1371/journal.pone.0133454
Starting Page	133454
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	8
Volume Number	10
Language	English
Publisher	Public Library of Science
Publisher Date	2015-08-01
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Agricultural and Biological Sciences(all) Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The Human Cathelicidin LL-37 Has Antiviral Activity against Respiratory Syncytial Virus

Structural and functional analysis of the pro-domain of human cathelicidin, LL-37

Structural and Functional Studies of Influenza Virus A/H6 Hemagglutinin

LL-37 modulates human neutrophil responses to influenza A virus

Functional Analysis of Conserved Motifs in Influenza Virus PB1 Protein

Guidelines for Identifying Homologous Recombination Events in Influenza A Virus

Vesicular LL-37 Contributes to Inflammation of the Lesional Skin of Palmoplantar Pustulosis

OmpA Binding Mediates the Effect of Antimicrobial Peptide LL-37 on Acinetobacter baumannii

Evaluation of the Ability of LL-37 to Neutralise LPS In Vitro and Ex Vivo

Identifying the Critical Domain of LL-37 Involved in Mediating Neutrophil Activation in the Presence of Influenza Virus: Functional and Structural Analysis

Similar Documents

The Human Cathelicidin LL-37 Has Antiviral Activity against Respiratory Syncytial Virus

Structural and functional analysis of the pro-domain of human cathelicidin, LL-37

Structural and Functional Studies of Influenza Virus A/H6 Hemagglutinin

LL-37 modulates human neutrophil responses to influenza A virus

Functional Analysis of Conserved Motifs in Influenza Virus PB1 Protein

Guidelines for Identifying Homologous Recombination Events in Influenza A Virus

Vesicular LL-37 Contributes to Inflammation of the Lesional Skin of Palmoplantar Pustulosis

OmpA Binding Mediates the Effect of Antimicrobial Peptide LL-37 on Acinetobacter baumannii

Evaluation of the Ability of LL-37 to Neutralise LPS In Vitro and Ex Vivo

Identifying the Critical Domain of LL-37 Involved in Mediating Neutrophil Activation in the Presence of Influenza Virus: Functional and Structural Analysis