Staphylococcus aureus alpha toxin activates Notch in vascular cells.
ADAM10 Protein
/ metabolism
Amyloid Precursor Protein Secretases
/ metabolism
Bacterial Proteins
/ chemistry
Bacterial Toxins
/ chemistry
Hemolysin Proteins
/ chemistry
Human Umbilical Vein Endothelial Cells
/ metabolism
Humans
Membrane Proteins
/ metabolism
Receptors, Notch
/ metabolism
Signal Transduction
/ drug effects
Staphylococcal Infections
/ metabolism
Staphylococcus aureus
/ chemistry
Alpha-toxin
HUVEC
Notch
Staphylococcus aureus
Journal
Angiogenesis
ISSN: 1573-7209
Titre abrégé: Angiogenesis
Pays: Germany
ID NLM: 9814575
Informations de publication
Date de publication:
02 2019
02 2019
Historique:
received:
09
01
2018
accepted:
24
09
2018
pubmed:
17
10
2018
medline:
27
3
2020
entrez:
17
10
2018
Statut:
ppublish
Résumé
Staphylococcus aureus infection is one of the leading causes of morbidity in hospitalized patients in the United States, an effect compounded by increasing antibiotic resistance. The secreted agent hemolysin alpha toxin (Hla) requires the receptor A Disintegrin And Metalloproteinase domain-containing protein 10 (ADAM10) to mediate its toxic effects. We hypothesized that these effects are in part regulated by Notch signaling, for which ADAM10 activation is essential. Notch proteins function in developmental and pathological angiogenesis via the modulation of key pathways in endothelial and perivascular cells. Thus, we hypothesized that Hla would activate Notch in vascular cells. Human umbilical vein endothelial cells were treated with recombinant Hla (rHla), Hla-H35L (genetically inactivated Hla), or Hank's solution (HBSS), and probed by different methods. Luciferase assays showed that Hla (0.01 µg/mL) increased Notch activation by 1.75 ± 0.5-fold as compared to HBSS controls (p < 0.05), whereas Hla-H35L had no effect. Immunocytochemistry and Western blotting confirmed these findings and revealed that ADAM10 and γ-secretase are required for Notch activation after inhibitor and siRNA assays. Retinal EC in mice engineered to express yellow fluorescent protein (YFP) upon Notch activation demonstrated significantly greater YFP intensity after Hla injection than controls. Aortic rings from Notch reporter mice embedded in matrix and incubated with rHla or Hla-H35L demonstrate increased Notch activation occurs at tip cells during sprouting. These mice also had higher skin YFP intensity and area of expression after subcutaneous inoculation of S. aureus expressing Hla than a strain lacking Hla in both EC and pericytes assessed by microscopy. Human liver displayed strikingly higher Notch expression in EC and pericytes during S. aureus infection by immunohistochemistry than tissues from uninfected patients. In sum, our results demonstrate that the S. aureus toxin Hla can potently activate Notch in vascular cells, an effect which may contribute to the pathobiology of infection with this microorganism.
Identifiants
pubmed: 30324336
doi: 10.1007/s10456-018-9650-5
pii: 10.1007/s10456-018-9650-5
pmc: PMC6360126
mid: NIHMS1509708
doi:
Substances chimiques
Bacterial Proteins
0
Bacterial Toxins
0
Hemolysin Proteins
0
Membrane Proteins
0
Receptors, Notch
0
Amyloid Precursor Protein Secretases
EC 3.4.-
ADAM10 Protein
EC 3.4.24.81
ADAM10 protein, human
EC 3.4.24.81
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
197-209Subventions
Organisme : NCI NIH HHS
ID : P30 CA014599
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI097434
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007197
Pays : United States
Références
Development. 2014 Jun;141(12):2446-51
pubmed: 24917500
Invest Ophthalmol Vis Sci. 2010 Jun;51(6):2813-26
pubmed: 20484600
Biochem Soc Trans. 2009 Dec;37(Pt 6):1221-7
pubmed: 19909251
J Innate Immun. 2014;6(5):619-31
pubmed: 24820433
J Infect Dis. 2012 Aug 1;206(3):352-6
pubmed: 22474035
Epidemiol Infect. 2017 Sep;145(12):2631-2639
pubmed: 28748772
Nature. 2006 Dec 21;444(7122):1083-7
pubmed: 17183323
PLoS One. 2007 Nov 14;2(11):e1167
pubmed: 18000539
Nature. 2007 Feb 15;445(7129):776-80
pubmed: 17259973
J Invest Dermatol. 2012 May;132(5):1513-6
pubmed: 22377761
Infect Control Hosp Epidemiol. 2016 Jul;37(7):782-90
pubmed: 27019995
Br J Cancer. 2008 Oct 21;99(8):1204-9
pubmed: 18827808
Nat Med. 2011 Sep 18;17(10):1310-4
pubmed: 21926978
Genes Dev. 1994 Mar 15;8(6):707-19
pubmed: 7926761
Dev Biol. 2015 Jun 1;402(1):98-108
pubmed: 25835502
Cancer Res. 2015 Apr 15;75(8):1592-602
pubmed: 25744722
Mol Cell Biol. 2000 Mar;20(5):1825-35
pubmed: 10669757
Int J Med Microbiol. 2011 Aug;301(6):500-5
pubmed: 21570348
Nat Protoc. 2011 Dec 22;7(1):89-104
pubmed: 22193302
Science. 1998 Nov 13;282(5392):1281-4
pubmed: 9812885
Hum Mol Genet. 2002 Oct 1;11(21):2615-24
pubmed: 12354787
Proc Natl Acad Sci U S A. 2010 Jul 27;107(30):13473-8
pubmed: 20624979
Nature. 2006 Dec 21;444(7122):1032-7
pubmed: 17183313
Genes Dev. 2000 Jun 1;14(11):1343-52
pubmed: 10837027
Cancer Discov. 2015 Feb;5(2):182-97
pubmed: 25387766
J Biol Chem. 2009 Nov 6;284(45):31018-27
pubmed: 19726682
Nature. 2010 Apr 15;464(7291):1052-7
pubmed: 20393564
J Biol Chem. 2001 Sep 14;276(37):34371-8
pubmed: 11425854
BMC Dev Biol. 2013 Apr 25;13:15
pubmed: 23617465
Development. 1996 Jul;122(7):2251-9
pubmed: 8681805
Development. 2012 Feb;139(3):488-97
pubmed: 22190634