PMID- 20605975
OWN - NLM
STAT- MEDLINE
DCOM- 20100913
LR  - 20240319
IS  - 1098-5522 (Electronic)
IS  - 0019-9567 (Print)
IS  - 0019-9567 (Linking)
VI  - 78
IP  - 9
DP  - 2010 Sep
TI  - Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen 
      and mediates interaction of yeast forms with host cells.
PG  - 4040-50
LID - 10.1128/IAI.00221-10 [doi]
AB  - Paracoccidioidomycosis (PCM), caused by the dimorphic fungus Paracoccidioides 
      brasiliensis, is a disseminated, systemic disorder that involves the lungs and 
      other organs. The ability of the pathogen to interact with host components, 
      including extracellular matrix (ECM) proteins, is essential to further 
      colonization, invasion, and growth. Previously, enolase (EC 4.2.1.11) was 
      characterized as a fibronectin binding protein in P. brasiliensis. Interaction of 
      surface-bound enolase with plasminogen has been incriminated in tissue invasion 
      for pathogenesis in several pathogens. In this paper, enolase was expressed in 
      Escherichia coli as a recombinant glutathione S-transferase (GST) fusion protein 
      (recombinant P. brasiliensis enolase [rPbEno]). The P. brasiliensis native 
      enolase (PbEno) was detected at the fungus surface and cytoplasm by 
      immunofluorescence with an anti-rPbEno antibody. Immobilized purified rPbEno 
      bound plasminogen in a specific, concentration-dependent fashion. Both native 
      enolase and rPbEno activated conversion of plasminogen to plasmin through tissue 
      plasminogen activator. The association between PbEno and plasminogen was lysine 
      dependent. In competition experiments, purified rPbEno, in its soluble form, 
      inhibited plasminogen binding to fixed P. brasiliensis, suggesting that this 
      interaction required surface-localized PbEno. Plasminogen-coated P. brasiliensis 
      yeast cells were capable of degrading purified fibronectin, providing in vitro 
      evidence for the generation of active plasmin on the fungus surface. Exposure of 
      epithelial cells and phagocytes to enolase was associated with an increased 
      expression of surface sites of adhesion. In fact, the association of P. 
      brasiliensis with epithelial cells and phagocytes was increased in the presence 
      of rPbEno. The expression of PbEno was upregulated in yeast cells derived from 
      mouse-infected tissues. These data indicate that surface-associated PbEno may 
      contribute to the pathogenesis of P. brasiliensis.
FAU - Nogueira, Sarah Veloso
AU  - Nogueira SV
AD  - Laboratorio de Biologia Molecular, Instituto de Ciencias Biologicas, ICBII, 
      Campus II, Universidade Federal de Goias, 74001-970, Goiania, Goias, Brazil.
FAU - Fonseca, Fernanda L
AU  - Fonseca FL
FAU - Rodrigues, Marcio L
AU  - Rodrigues ML
FAU - Mundodi, Vasanth
AU  - Mundodi V
FAU - Abi-Chacra, Erika A
AU  - Abi-Chacra EA
FAU - Winters, Michael S
AU  - Winters MS
FAU - Alderete, John F
AU  - Alderete JF
FAU - de Almeida Soares, Celia Maria
AU  - de Almeida Soares CM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100706
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 9001-91-6 (Plasminogen)
RN  - EC 4.2.1.11 (Phosphopyruvate Hydratase)
SB  - IM
MH  - Animals
MH  - Female
MH  - Fibrinolysis
MH  - Humans
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Paracoccidioides/*physiology
MH  - Paracoccidioidomycosis/etiology
MH  - Phosphopyruvate Hydratase/immunology/*physiology
MH  - Plasminogen/*metabolism
MH  - Rabbits
PMC - PMC2937444
EDAT- 2010/07/08 06:00
MHDA- 2010/09/14 06:00
PMCR- 2011/03/01
CRDT- 2010/07/08 06:00
PHST- 2010/07/08 06:00 [entrez]
PHST- 2010/07/08 06:00 [pubmed]
PHST- 2010/09/14 06:00 [medline]
PHST- 2011/03/01 00:00 [pmc-release]
AID - IAI.00221-10 [pii]
AID - 0221-10 [pii]
AID - 10.1128/IAI.00221-10 [doi]
PST - ppublish
SO  - Infect Immun. 2010 Sep;78(9):4040-50. doi: 10.1128/IAI.00221-10. Epub 2010 Jul 6.