VFG011430
Help to interpret the results
Three outputs have been generated:
General: this tab contains the description, occurence in the database and other information related to the selected Virulence factor VFG011430
Protein list: lists the 7 occurences of the Virulence factor within the database. The table reports information on each occurence.
Profile: phylogenetic tree annotated with
- the presence of the Virulence factor of interest within all the genomes of the database (first column)
- the size of the orthogroup(s) in which the reported Virulence factor has been clustered.
Orthogroups are shown in red if they are annotated with that particular Virulence factor in a given genome , in green otherwise, i.e. if there is a discrepency between orthogroup clustering and Virulence factor prediction.
Green homologs (same orthogroup) are not positive hit(s) for the considered Virulence factor.
Variations within orthogroups may be due to the clustering of multi domain proteins or because of erroneous homolog clustering or Virulence factor prediction.
Description
| Protein |
acyl carrier protein |
| VF ID |
VF0367 |
| Category |
Immune modulation |
| Protein ID |
WP_002963616 |
| Characteristics |
Brucella possesses a non-classical LPS as compared with the so-called classical LPS from enterobacteria such as Escherichia coli. B. abortus lipid A possesses a diaminoglucose backbone (rather than glucosamine), and acyl groups are longer (C28 rather than C12 and C16) and are only linked to the core by amide bounds (rather than ester and amide bonds).; In contrast to enterobacterial LPSs, Brucella LPS is several-hundred-times less active and toxic than E. coli LPS.; this is an evolutionary adaptation to an intracellular lifestyle, low endotoxic activity is shared by other intracellular pathogens such as Bartonella and Legionella. |
| Function |
Plays a role in entry and early survival inside macrophages; Resistance to innate-immunity anti-bacterial responses; a modulator of the immune response |
| Mechanism |
The entry and early survival stages of smooth Brucella are lipid-raft-dependent. The entry-gateway seems to include Brucella surface-exposed HSP60-PrPc (cellular prion protein) interaction but also a SR-A (class A scavenger)-lipid-A interaction and is also dependent on the LPS O-chain. And the LPS O-chain ensures the Brucella containing vacuole (BCV) aviodance of fusion with lysosomes transiently; The chemical structure of Brucella LPS permits the bacteria to become highly resistant to anti-bacterial effectors of the innate immune system. Long O-chains at the bacterial surface should provoke a steric hindrance leading to the formation of a protecting barrier. The presence of long O-chains at the surface of Brucella prevents the deposition of complement at the bacterial surface. The O-chains also could prevent a specific recognition of the Pathogen-associated molecular patterns (PAMPs) and as a consequence impair expression of any cytokines or iNOS, both of which are known to be involved in the clearance of intracellular Brucella. The low number of anionic groups in the core lipid A, especially charged phosphate groups could both remove anionic targets and facilitate a tighter aggregation of LPS molecules via their hydrophobic fatty acids, leading to less binding and penetration of antibacterial cationic peptides.;The Brucella LPS forms stable large clusters with MHC-II named macrodomians in the cell surface, interfering with MHC-II presentation of peptides to specific CD4+ T cells. |
| Vf_category_id |
VFC0258 |
Occurence in the database
| VFG011430 is associated with 7 different
proteins
|
|
The 7 proteins are classified into 1 different orthogroup(s)
|
