A5078179327- Toxin Mechanisms and Immunotoxins
- Cell death mechanisms and regulation
- Bacterial Genetics and Biotechnology
- Yersinia bacterium, plague, ectoparasites research
- Aquaculture disease management and microbiota
- Redox biology and oxidative stress
- Archaeology and Rock Art Studies
- Bacillus and Francisella bacterial research
- NF-κB Signaling Pathways
- Forensic and Genetic Research
- Nicotinic Acetylcholine Receptors Study
- bioluminescence and chemiluminescence research
- Linguistics and Language Studies
- Streptococcal Infections and Treatments
- Race, Genetics, and Society
- Connexins and lens biology
- Heat shock proteins research
- Vibrio bacteria research studies
- Natural Language Processing Techniques
Universidade do Porto
2002-2023
i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto
2019
AIP56 (apoptosis-inducing protein of 56 kDa) is a major virulence factor Photobacterium damselae piscicida (Phdp), Gram-negative pathogen that causes septicemic infections, which are among the most threatening diseases in mariculture. The toxin triggers apoptosis host macrophages and neutrophils through process that, vivo, culminates with secondary necrosis apoptotic cells contributing to necrotic lesions observed diseased animals. Here, we show NF-κB p65-cleaving zinc-metalloprotease whose...
Ancient diversity in Sub‐Saharan Africa is known to have been re‐modulated a large extent by Bantu migrations the sub‐Sahel region, two southwards waves of advance through both west and east coasts. Haplotype matching performed for Y‐STR haplotypes several sub‐Saharan populations, inside outside migration path, allowed confirmation putative founder haplotype, its one‐step neighbours, origin, detected an increasing drift towards south, with stronger reduction along western coast. A mixed...
Abstract Bacterial AB toxins are secreted key virulence factors that internalized by target cells through receptor-mediated endocytosis, translocating their enzymatic domain to the cytosol from endosomes (short-trip) or endoplasmic reticulum (long-trip). To accomplish this, bacterial evolved a multidomain structure organized into either single polypeptide chain non-covalently associated chains. The prototypical short-trip single-chain toxin is characterized receptor-binding confers cellular...
ABSTRACT AIP56 (apoptosis-inducing protein of 56 kDa) is a metalloprotease AB toxin secreted by Photobacterium damselae subsp. piscicida that acts cleaving NF-κB. During infection, spreads systemically and depletes phagocytes postapoptotic secondary necrosis, impairing the host phagocytic defense contributing to genesis infection-associated necrotic lesions. Here we show mouse bone marrow-derived macrophages (mBMDM) intoxicated undergo NF-κB p65 depletion apoptosis. Similarly what was...
Abstract AIP56 (apoptosis inducing protein of 56 kDa) is a key virulence factor secreted by virulent strains Photobacterium damselae subsp. piscicida ( Phdp ), Gram-negative bacterium that causes septicemic infections in several warm water marine fish species. systemically disseminated during infection and induces massive apoptosis host macrophages neutrophils, playing decisive role the disease outcome. single-chain AB-type toxin, being composed metalloprotease A domain located at N-terminal...
Apoptosis-inducing protein of 56 kDa (AIP56) is a major virulence factor Photobacterium damselae subsp. piscicida, gram-negative pathogen that infects warm water fish species worldwide and causes serious economic losses in aquacultures. AIP56 single-chain AB toxin composed by two domains connected an unstructured linker peptide flanked cysteine residues form disulphide bond. The A domain comprises zinc-metalloprotease moiety cleaves the NF-kB p65, B involved binding internalisation into...
ABSTRACT Bacterial AB toxins are secreted virulence factors that internalized by target cells through receptor-mediated endocytosis, translocating their enzymatic domain to the cytosol from endosomes (short-trip) or endoplasmic reticulum (long-trip). To accomplish this, they evolved a multidomain structure organized into either single polypeptide chain non-covalently associated chains. The prototypical short-trip single-chain toxin is characterized receptor-binding confers cellular...