unique proteins present only in B.cereus

Introduction

Bacillus cereus is a Gram-positive bacterium known for causing foodborne illnesses and other infections. It is part of the B. cereus group, which includes closely related species such as B. anthracis and B. thuringiensis. Identifying unique proteins in B. cereus is crucial for understanding its pathogenic mechanisms and differentiating it from other species in the group.

Key Insights

IlsA Protein for Iron Acquisition:
- IlsA is a unique surface protein in B. cereus essential for iron acquisition from hemoglobin, heme, and ferritin, contributing to its virulence.
Characteristic Proteins by Molecular Weight:
- B. cereus has three characteristic proteins with molecular weights approximately 28.5, 26.5, and 20 kDa, which are not found in B. thuringiensis, B. megaterium, or B. mycoides.
Enterotoxic Protein bceT:
- The bceT gene encodes an enterotoxic protein causing diarrheal symptoms, which is unique to B. cereus and contributes to its pathogenicity.
Small Acid-Soluble Spore Proteins (SASP):
- SASP alpha and beta in B. cereus show minor amino acid substitutions compared to B. anthracis, making them useful biomarkers for differentiation within the B. cereus group.
LmbE Family Proteins:
- B. cereus contains LmbE family proteins (BC1534 and BC3461) with broad substrate specificity, which are highly similar to those in B. anthracis but still distinct in their biochemical properties.
Zinc-Binding Protein (BcZBP):
- BcZBP is a zinc-binding protein in B. cereus with deacetylase activity, structurally similar to zinc-dependent hydrolases but unique in its specific substrate interactions.
EntD Protein:
- EntD is a pivotal protein in B. cereus for the production of numerous virulence factors, affecting central metabolism, cell structure, motility, and toxin production.

Conclusion

Bacillus cereus possesses several unique proteins that contribute to its pathogenicity and differentiate it from other species in the B. cereus group. Key proteins include IlsA for iron acquisition, characteristic proteins by molecular weight, the enterotoxic protein bceT, SASP alpha and beta, LmbE family proteins, the zinc-binding protein BcZBP, and the pivotal virulence factor EntD. These proteins play crucial roles in the bacterium's ability to cause disease and adapt to various environments.

Try another search

What are the symptoms of bruxism?

How is heart disease diagnosed and treated?

What are the latest findings on the health effects of long-term low-dose radiation exposure?

what are hyenas related to

How can I manage lactose intolerance?

How can the principles of biomechanics be applied to improve exercise technique and prevent injuries?

Unique proteins present only in B.cereus

Summary

Introduction

Key Insights

Conclusion

Sources and full results

IlsA, A Unique Surface Protein of Bacillus cereus Required for Iron Acquisition from Heme, Hemoglobin and Ferritin

IlsA, a novel Bacillus cereus surface protein, is essential for iron acquisition from hemoglobin, heme, and ferritin, playing a key role in the pathogen's virulence strategy to colonize susceptible hosts.

Isolation and Purification of Characteristic Proteins of Bacillus cereus

Bacillus cereus has three distinct characteristic proteins with molecular weights of 28.5,26.520 KDa, while B.thuringiensis, B.megaterium, and B.mycoides do not.

The bceT gene of Bacillus cereus encodes an enterotoxic protein.

The bceT gene encodes one of Bacillus cereus' enterotoxic proteins, which cause food-borne diarrhoea and are characteristic of diarrhoeal enterotoxins.

The small acid soluble proteins (SASP alpha and SASP beta) of Bacillus weihenstephanensis and Bacillus mycoides group 2 are the most distinct among the Bacillus cereus group.

Bacillus weihenstephanensis and Bacillus mycoides group 2 have distinct small acid soluble proteins, making them unique taxonomic discriminators within the Bacillus cereus group.

LmbE proteins from Bacillus cereus are de‐N‐acetylases with broad substrate specificity and are highly similar to proteins in Bacillus anthracis

Bacillus cereus LmbE proteins show broad substrate specificity and are highly similar to Bacillus anthracis LmbE proteins, with potential applications in drug discovery and bacterial pathogenesis.

Crystal structure of the BcZBP, a zinc‐binding protein from Bacillus cereus

The crystal structure of BcZBP, a zinc-binding protein from Bacillus cereus, reveals similarities to MshB and LpxC, suggesting a potential catalytic mechanism and function in anthrax pathogenesis.

Proteomics identifies Bacillus cereus EntD as a pivotal protein for the production of numerous virulence factors

Bacillus cereus EntD is a key protein involved in virulence, contributing to central metabolism, cell structure, antioxidative ability, cell motility, and toxin production.

Cloning and nucleotide sequencing of genes for a second type of small, acid-soluble spore proteins of Bacillus cereus, Bacillus stearothermophilus, and "Thermoactinomyces thalpophilus"

The B-type small, acid-soluble spore proteins (SASP) of Bacillus cereus, B. stearothermophilus, and "Thermoactinomyces thalpophilus" show significant sequence conservation, but only 19 residues are exactly conserved across all five proteins.

A new Bacillus cereus DNA-binding protein, HlyIIR, negatively regulates expression of B. cereus haemolysin II.

HlyIIR, a new Bacillus cereus gene, negatively regulates haemolysin II expression in Escherichia coli cells, potentially impacting foodborne pathogen's haemolytic activity.

The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1.

Bacillus cereus ATCC 10987 has unique metabolic capabilities and a large pXO1-like plasmid, making it a potential model for studying B.anthracis plasmid biology and regulatory cross-talk.

Try another search