scholarly journals Brucella abortus Encodes an Active Rhomboid Protease: Proteome Response after Rhomboid Gene Deletion

2022 ◽  
Vol 10 (1) ◽  
pp. 114
Author(s):  
María Inés Marchesini ◽  
Ansgar Poetsch ◽  
Leticia Soledad Guidolín ◽  
Diego J. Comerci

Rhomboids are intramembrane serine proteases highly conserved in the three domains of life. Their key roles in eukaryotes are well understood but their contribution to bacterial physiology is still poorly characterized. Here we demonstrate that Brucella abortus, the etiological agent of the zoonosis called brucellosis, encodes an active rhomboid protease capable of cleaving model heterologous substrates like Drosophila melanogaster Gurken and Providencia stuartii TatA. To address the impact of rhomboid deletion on B. abortus physiology, the proteomes of mutant and parental strains were compared by shotgun proteomics. About 50% of the B. abortus predicted proteome was identified by quantitative proteomics under two experimental conditions and 108 differentially represented proteins were detected. Membrane associated proteins that showed variations in concentration in the mutant were considered as potential rhomboid targets. This class included nitric oxide reductase subunit C NorC (Q2YJT6) and periplasmic protein LptC involved in LPS transport to the outer membrane (Q2YP16). Differences in secretory proteins were also addressed. Differentially represented proteins included a putative lytic murein transglycosylase (Q2YIT4), nitrous-oxide reductase NosZ (Q2YJW2) and high oxygen affinity Cbb3-type cytochrome c oxidase subunit (Q2YM85). Deletion of rhomboid had no obvious effect in B. abortus virulence. However, rhomboid overexpression had a negative impact on growth under static conditions, suggesting an effect on denitrification enzymes and/or high oxygen affinity cytochrome c oxidase required for growth in low oxygen tension conditions.

1975 ◽  
Vol 400 (2) ◽  
pp. 343-347 ◽  
Author(s):  
H.B. Kleckner ◽  
J.B. Wilson ◽  
J.G. Lindeman ◽  
P.D. Stevens ◽  
G. Niazi ◽  
...  

1995 ◽  
Vol 96 (6) ◽  
pp. 711-716 ◽  
Author(s):  
H. Wajcman ◽  
E. Girodon ◽  
D. Prom� ◽  
M.L. North ◽  
F. Plassa ◽  
...  

Author(s):  
Epifania Rita Testa ◽  
Adriana Masotti ◽  
Patrizia Valeri ◽  
Luciana Geremia ◽  
Valeria Brunetta ◽  
...  

Author(s):  
Abhay A Bhave ◽  
Lakshmi Iyer ◽  
Nawal Kazi ◽  
Manju Gorivale ◽  
Anita Nadkarni

High oxygen affinity haemoglobin variants are rare and often underdiagnosed in persistent erythrocytosis with no apparent aetiology. Here the author present a 29-year-old Indian male patient with a long-standing history of erythrocytosis which was incidentally detected. The proband had a prothrombotic family history of cerebral vessel stroke in his paternal grandfather at a young age and unexplained erythrocytosis in his father and brother. A review of his haemograms showed persistent high haemoglobin values. Routine tests did not reveal any specific aetiology and haemoglobin electrophoresis by High-Performance Liquid Chromatography (HPLC) showed absence of any abnormal peak or unstable haemoglobin. DNA sequencing of the β globin gene revealed heterozygosity for codon 20 {GTG→ATG, Valine (Val)→ Methionine (Met)} mutation confirming the presence of an electrophoretically silent Hb variant - Haemoglobin Olympia in him and his extended family members. This case study emphasises importance of this rare entity of high oxygen affinity haemoglobin variant as a differential diagnosis while screening for erythrocytosis. This is the first case report of Haemoglobin Olympia from India reported in the literature.


2016 ◽  
Vol 55 (3) ◽  
pp. 285-287
Author(s):  
Raku Son ◽  
Takakazu Higuchi ◽  
Atsushi Mizuno ◽  
Ryosuke Koyamada ◽  
Sadamu Okada ◽  
...  

Hemoglobin ◽  
2020 ◽  
Vol 44 (1) ◽  
pp. 10-12
Author(s):  
Ibrahim Al Nabhani ◽  
John C. Aneke ◽  
Madeleine Verhovsek ◽  
Barry Eng ◽  
Kevin H.M. Kuo ◽  
...  

Blood ◽  
1979 ◽  
Vol 54 (1) ◽  
pp. 54-63 ◽  
Author(s):  
A Maniatis ◽  
T Bousios ◽  
RL Nagel ◽  
T Balazs ◽  
Y Ueda ◽  
...  

Abstract Hemoglobin Crete, beta129 (h7)ala leads to pro, is a new mutant hemoglobin (Hb) with high oxygen affinity that was discovered in a Greek family in various combinations with beta- and deltabeta- thalassemia. The propositus, who presented an unusual clinical picture of an “overcompensated” hemolytic state, with erythrocytosis, splenomegaly, abnormal red cell morphology, and marked erythroid hyperplasia, appeared doubly heterozygous for Hb Crete and deltabeta- thalassemia. His red cells contained 67% Hb Crete and 30% Hb F, and the combination of these two hemoglobins resulted in a blood P50O2 of 11.2 mm Hg. A brother with Hb Crete trait (38% Hb Crete, 56% Hb A, blood P50O2 23.0 mm Hg) did not have significant erythrocytosis. Purified Hb Crete was heat-unstable and exhibited a high oxygen affinity, and a normal Bohr effect. We postulate that the beta 129 proline substitution disrupts the H helix, perturbing nearby residues involved in alpha 1 beta 1 contact sites of the Hb tetramer.


2002 ◽  
Vol 108 (3) ◽  
pp. 132-138 ◽  
Author(s):  
O. David ◽  
G. Ivaldi ◽  
E. Rabino-Massa ◽  
G. Ricco

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