The Laminin Interactome : A Multifactorial Laminin-Binding Strategy by Nontypeable Haemophilus influenzae for Effective Adherence and Colonization
Su, Shanice Yc LU ; Mattsson, Emma LU ; Singh, Birendra LU ; Jalalvand, Farshid LU ; Murphy, Timothy F. and Riesbeck, Kristian LU
(2019)
In The Journal of infectious diseases
220(6).
p.1049-1060
- Abstract
Laminin is a well-defined component of the airway basement membrane (BM). Efficient binding of laminin via multiple interactions is important for nontypeable Haemophilusinfluenzae (NTHi) colonization in the airway mucosa. Here we identified elongation factor thermo-unstable (EF-Tu), L-lactate dehydrogenase (LDH), Protein D and peptidoglycan-associated lipoprotein P6 as novel laminin-binding proteins (Lbps) of NTHi. In parallel with other well-studied Lbps (P4, PE, PF and Hap), EF-Tu, LDH, PD and P6 exhibited interactions with laminin, and mediated NTHi laminin-dependent adherence to pulmonary epithelial cell lines. Importantly, the NTHi laminin interactome consisting of the well-studied and novel Lbps recognized laminin LG domains from... (More)
Laminin is a well-defined component of the airway basement membrane (BM). Efficient binding of laminin via multiple interactions is important for nontypeable Haemophilusinfluenzae (NTHi) colonization in the airway mucosa. Here we identified elongation factor thermo-unstable (EF-Tu), L-lactate dehydrogenase (LDH), Protein D and peptidoglycan-associated lipoprotein P6 as novel laminin-binding proteins (Lbps) of NTHi. In parallel with other well-studied Lbps (P4, PE, PF and Hap), EF-Tu, LDH, PD and P6 exhibited interactions with laminin, and mediated NTHi laminin-dependent adherence to pulmonary epithelial cell lines. Importantly, the NTHi laminin interactome consisting of the well-studied and novel Lbps recognized laminin LG domains from the subunit α chains of laminin-111 and -332, of which the latter isoform is the main laminin in the airway BM. The NTHi interactome mainly targeted multiple heparin-binding domains of laminin. In conclusion, the NTHi interactome exhibited a high plasticity of interactions with different laminin isoforms via multiple heparin-binding sites.
(Less)
- author
- Su, Shanice Yc
LU
; Mattsson, Emma
LU
; Singh, Birendra
LU
; Jalalvand, Farshid
LU
; Murphy, Timothy F.
and Riesbeck, Kristian
LU
- organization
- publishing date
- 2019-04-29
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of infectious diseases
- volume
- 220
- issue
- 6
- pages
- 1049 - 1060
- publisher
- Oxford University Press
- external identifiers
-
- scopus:85071347636
- pmid:31034569
- ISSN
- 1537-6613
- DOI
- 10.1093/infdis/jiz217
- language
- English
- LU publication?
- yes
- additional info
- © The Author(s) 2019. Published by Oxford University Press for the Infectious Diseases Society of America. All rights reserved. For permissions, e-mail: journals.permissions@oup.com.
- id
- 6cf3390c-7079-41b2-a777-38e4c14d5fe5
- date added to LUP
- 2019-06-07 15:38:03
- date last changed
- 2024-05-28 14:59:59
@article{6cf3390c-7079-41b2-a777-38e4c14d5fe5,
abstract = {{<p>Laminin is a well-defined component of the airway basement membrane (BM). Efficient binding of laminin via multiple interactions is important for nontypeable Haemophilusinfluenzae (NTHi) colonization in the airway mucosa. Here we identified elongation factor thermo-unstable (EF-Tu), L-lactate dehydrogenase (LDH), Protein D and peptidoglycan-associated lipoprotein P6 as novel laminin-binding proteins (Lbps) of NTHi. In parallel with other well-studied Lbps (P4, PE, PF and Hap), EF-Tu, LDH, PD and P6 exhibited interactions with laminin, and mediated NTHi laminin-dependent adherence to pulmonary epithelial cell lines. Importantly, the NTHi laminin interactome consisting of the well-studied and novel Lbps recognized laminin LG domains from the subunit α chains of laminin-111 and -332, of which the latter isoform is the main laminin in the airway BM. The NTHi interactome mainly targeted multiple heparin-binding domains of laminin. In conclusion, the NTHi interactome exhibited a high plasticity of interactions with different laminin isoforms via multiple heparin-binding sites.</p>}},
author = {{Su, Shanice Yc and Mattsson, Emma and Singh, Birendra and Jalalvand, Farshid and Murphy, Timothy F. and Riesbeck, Kristian}},
issn = {{1537-6613}},
language = {{eng}},
month = {{04}},
number = {{6}},
pages = {{1049--1060}},
publisher = {{Oxford University Press}},
series = {{The Journal of infectious diseases}},
title = {{The Laminin Interactome : A Multifactorial Laminin-Binding Strategy by Nontypeable Haemophilus influenzae for Effective Adherence and Colonization}},
url = {{http://dx.doi.org/10.1093/infdis/jiz217}},
doi = {{10.1093/infdis/jiz217}},
volume = {{220}},
year = {{2019}},
}