scholarly journals Characterization of the IgA1 protease from the Brazilian purpuric fever strain F3031 ofHaemophilus influenzaebiogroup aegyptius

2005 ◽  
Vol 250 (2) ◽  
pp. 229-236 ◽  
Author(s):  
Glen McGillivary ◽  
Laura M. Smoot ◽  
Luis A. Actis
2000 ◽  
Vol 38 (7) ◽  
pp. 2760-2762 ◽  
Author(s):  
Jeanet A. Lomholt ◽  
Mogens Kilian

The purpose of this study was to determine the occurrence and nature of immunoglobulin A1 (IgA1) protease activity in members of the genus Gemella and related taxa. Among a total of 22Gemella strains belonging to the four species Gemella haemolysans, Gemella morbillorum, Gemella sanguinis, and Gemella bergeriae and four reference strains of the species Helcococcus kunzii, Facklamia hominis, and Globicatella sanguinis, IgA1 protease activity was an exclusive character of all nine isolates of G. haemolysans. The IgA1 protease of G. haemolysansappears to be a metallo-type IgA1 protease that cleaves the Pro227-Thr228 peptide bond in the hinge region of the α1 chain like that of several Streptococcusspecies. Phenotypic characterization of the isolates demonstrates that screening for IgA1 protease activity provides a valuable means for species differentiation in this group of bacteria.


2010 ◽  
Vol 140 (1-2) ◽  
pp. 171-175 ◽  
Author(s):  
Anding Zhang ◽  
Xiaofeng Mu ◽  
Bo Chen ◽  
Cheng Liu ◽  
Li Han ◽  
...  

1998 ◽  
Vol 188 (6) ◽  
pp. 1091-1103 ◽  
Author(s):  
Ben R. Otto ◽  
Silvy J.M. van Dooren ◽  
Jan H. Nuijens ◽  
Joen Luirink ◽  
Bauke Oudega

Many pathogenic bacteria can use heme compounds as a source of iron. Pathogenic Escherichia coli strains are capable of using hemoglobin as an iron source. However, the mechanism of heme acquisition from hemoglobin is not understood for this microorganism. We present the first molecular characterization of a hemoglobin protease (Hbp) from a human pathogenic E. coli strain. The enzyme also appeared to be a heme-binding protein. Affinity purification of this bifunctional protein enabled us to identify the extracellular gene product, and to clone and analyze its gene. A purification procedure developed for Hbp allowed us to perform functional studies. The protein interacted with hemoglobin, degraded it and subsequently bound the released heme. These results suggest that the protein is involved in heme acquisition by this human pathogen. Hbp belongs to the so-called IgA1 protease-like proteins, as indicated by the kinetics of its membrane transfer and DNA sequence similarity. The gene of this protein appears to be located on the large pColV-K30 episome, that only has been isolated from human and animal pathogens. All these characteristics indicate that Hbp may be an important virulence factor that may play a significant role in the pathogenesis of E. coli infections.


2000 ◽  
Vol 28 (3) ◽  
pp. 145-155 ◽  
Author(s):  
Lynn M. Segada ◽  
George M. Carlone ◽  
Linda L. Gheesling ◽  
Alan J. Lesse

2016 ◽  
Vol 18 (4) ◽  
pp. 285-289 ◽  
Author(s):  
Lei Fu ◽  
Jianqing Zhao ◽  
Lan Lin ◽  
Qiang Zhang ◽  
Zhongmin Xu ◽  
...  

2008 ◽  
Vol 21 (4) ◽  
pp. 594-605 ◽  
Author(s):  
Lee H. Harrison ◽  
Vera Simonsen ◽  
Eliseu A. Waldman

SUMMARY In 1984, children presented to the emergency department of a hospital in the small town of Promissão, São Paulo State, Brazil, with an acute febrile illness that rapidly progressed to death. Local clinicians and public health officials recognized that these children had an unusual illness, which led to outbreak investigations conducted by Brazilian health officials in collaboration with the U.S. Centers for Disease Control and Prevention. The studies that followed are an excellent example of the coordinated and parallel studies that are used to investigate outbreaks of a new disease, which became known as Brazilian purpuric fever (BPF). In the first outbreak investigation, a case-control study confirmed an association between BPF and antecedent conjunctivitis but the etiology of the disease could not be determined. In a subsequent outbreak, children with BPF were found to have bacteremia caused by Haemophilus influenzae biogroup aegyptius (H. aegyptius), an organism previously known mainly to cause self-limited purulent conjunctivitis. Molecular characterization of blood and other isolates demonstrated the clonal nature of the H. aegyptius strains that caused BPF, which were genetically distant from the diverse strains that cause only conjunctivitis. This led to an intense effort to identify the factors causing the unusual invasiveness of the BPF clone, which has yet to definitively identify the virulence factor or factors involved. After a series of outbreaks and sporadic cases through 1993, no additional cases of BPF have been reported.


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