Proteomic Characterization of a Natural Host–Pathogen Interaction: Repertoire of in Vivo Expressed Bacterial and Host Surface-Associated Proteins

2014 ◽  
Vol 14 (1) ◽  
pp. 120-132 ◽  
Author(s):  
Megan A. Rees ◽  
Oded Kleifeld ◽  
Paul K. Crellin ◽  
Bosco Ho ◽  
Timothy P. Stinear ◽  
...  
Keyword(s):  
Natural Host ◽  
Host Pathogen Interaction ◽  
Host Pathogen ◽  
Associated Proteins

scholarly journals In vivo host-pathogen interaction as revealed by global proteomic profiling of zebrafish larvae

2017 ◽  
Author(s):  
Francisco Díaz-Pascual ◽  
Javiera Ortíz-Severín ◽  
Macarena A. Varas ◽  
Miguel L. Allende ◽  
Francisco P. Chávez
Keyword(s):  
Microbial Pathogens ◽  
Cytokine Signaling ◽  
Proteomic Profiling ◽  
Zebrafish Larvae ◽  
Host Pathogen Interaction ◽  
Host Pathogen ◽  
Associated Proteins ◽  
Static Immersion

AbstractThe outcome of a host-pathogen interaction is determined by the conditions of the host, the pathogen, and the environment. Although numerous proteomic studies of in vitro-grown microbial pathogens have been performed, in vivo proteomic approaches are still rare. In addition, increasing evidence supports that in vitro studies inadequately reflect in vivo conditions. Choosing the proper host is essential to detect the expression of proteins from the pathogen in vivo. Numerous studies have demonstrated the suitability of zebrafish (Danio rerio) embryos as a model to in vivo studies of Pseudomonas aeruginosa infection. In most zebrafish-pathogen studies, infection is achieved by microinjection of bacteria into the larvae. However, few reports using static immersion of bacterial pathogens have been published. In this study we infected 3 days post-fertilization (DPF) zebrafish larvae with P. aeruginosa PAO1 by immersion and injection and tracked the in vivo immune response by the zebrafish. Additionally, by using non-isotopic (Q-exactive) metaproteomics we simultaneously evaluated the proteomic response of the pathogen (P. aeruginosa PAO1) and the host (zebrafish). We found some zebrafish metabolic pathways, such as hypoxia response via HIF activation pathway, exclusively enriched in the larvae exposed by static immersion. In contrast, we found that inflammation mediated by chemokine and cytokine signaling pathways was exclusively enriched in the larvae exposed by injection, while the integrin signaling pathway and angiogenesis were solely enriched in the larvae exposed by immersion. We also found important virulence factors from P. aeruginosa that were enriched only after exposure by injection, such as the Type-III secretion system and flagella-associated proteins. On the other hand, P. aeruginosa proteins involved in processes like biofilm formation, cellular responses to antibiotic and starvation were enriched exclusively after an exposure by immersion.We demonstrated the suitability of zebrafish embryos as a model for in vivo host-pathogen based proteomic studies in P. aeruginosa. Our global proteomic profiling identifies novel molecular signatures that give systematic insight into zebrafish-Pseudomonas interaction.

scholarly journals Establishment of Myotis myotis Cell Lines - Model for Investigation of Host-Pathogen Interaction in a Natural Host for Emerging Viruses

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e109795 ◽  
Author(s):  
Xiaocui He ◽  
Tomáš Korytář ◽  
Yaqing Zhu ◽  
Jiří Pikula ◽  
Hana Bandouchova ◽  
...  
Keyword(s):  
Cell Lines ◽  
Natural Host ◽  
Emerging Viruses ◽  
Host Pathogen Interaction ◽  
Myotis Myotis ◽  
Host Pathogen

scholarly journals Functional characterization of the collagen-binding protein DIP2093 and its influence on host–pathogen interaction and arthritogenic potential of Corynebacterium diphtheriae

Microbiology ◽  
2017 ◽  
Vol 163 (5) ◽  
pp. 692-701 ◽  
Author(s):  
Renata Stavracakis Peixoto ◽  
Camila Azevedo Antunes ◽  
Liliane Simpson Lourêdo ◽  
Vanilda Gonçalves Viana ◽  
Cintia Silva dos Santos ◽  
...  
Keyword(s):  
Binding Protein ◽  
Functional Characterization ◽  
Corynebacterium Diphtheriae ◽  
Collagen Binding ◽  
Host Pathogen Interaction ◽  
Host Pathogen

scholarly journals GENETIC VARIATION IN RESISTANCE AND FECUNDITY TOLERANCE IN A NATURAL HOST-PATHOGEN INTERACTION

Evolution ◽  
2014 ◽  
pp. n/a-n/a ◽  
Author(s):  
Benjamin J. Parker ◽  
Justine R. Garcia ◽  
Nicole M. Gerardo
Keyword(s):  
Genetic Variation ◽  
Natural Host ◽  
Host Pathogen Interaction ◽  
Host Pathogen

scholarly journals Alf1p, a CLIP-170 Domain-containing Protein, Is Functionally and Physically Associated with α-Tubulin

1999 ◽  
Vol 144 (1) ◽  
pp. 113-124 ◽  
Author(s):  
Becket Feierbach ◽  
Eva Nogales ◽  
Kenneth H. Downing ◽  
Tim Stearns
Keyword(s):  
Fluorescent Protein ◽  
Null Alleles ◽  
Microtubule Associated Proteins ◽  
Cytoplasmic Face ◽  
Associated Proteins ◽  
Green Fluorescent ◽  
Β Tubulin

Tubulin is a heterodimer of α- and β-tubulin polypeptides. Assembly of the tubulin heterodimer in vitro requires the CCT chaperonin complex, and a set of five proteins referred to as the tubulin cofactors (Tian, F., Y. Huang, H. Rommelaere, J. Vandekerckhove, C. Ampe, and N.J. Cowan. 1996. Cell. 86:287–296; Tian, G., S.A. Lewis, B. Feierbach, T. Stearns, H. Rommelaere, C. Ampe, and N.J. Cowan. 1997. J. Cell Biol. 138:821–832). We report the characterization of Alf1p, the yeast ortholog of mammalian cofactor B. Alf1p interacts with α-tubulin in both two-hybrid and immunoprecipitation assays. Alf1p and cofactor B contain a single CLIP-170 domain, which is found in several microtubule-associated proteins. Mutation of the CLIP-170 domain in Alf1p disrupts the interaction with α-tubulin. Mutations in α-tubulin that disrupt the interaction with Alf1p map to a domain on the cytoplasmic face of α-tubulin; this domain is distinct from the region of interaction between α-tubulin and β-tubulin. Alf1p-green fluorescent protein (GFP) is able to associate with microtubules in vivo, and this localization is abolished either by mutation of the CLIP-170 domain in Alf1p, or by mutation of the Alf1p-binding domain in α-tubulin. Analysis of double mutants constructed between null alleles of ALF1 and PAC2, which encodes the other yeast α-tubulin cofactor, suggests that Alf1p and Pac2p act in the same pathway leading to functional α-tubulin. The phenotype of overexpression of ALF1 suggests that Alf1p can act to sequester α-tubulin from interaction with β-tubulin, raising the possibility that it plays a regulatory role in the formation of the tubulin heterodimer.

scholarly journals Identification and Functional Characterization of Xanthomonas oryzae Pv. oryzae Isolates

2020 ◽  
pp. 78-84
Author(s):  
Diksha Kumari ◽  
Bishun Deo Parasad ◽  
Sangita Sahni ◽  
Abhijeet Ghatak
Keyword(s):  
Antioxidant Enzymes ◽  
Virulent Strain ◽  
Functional Characterization ◽  
Xanthomonas Oryzae ◽  
Host Pathogen Interaction ◽  
Ncbi Accession ◽  
Host Pathogen ◽  
Rice Leaves ◽  
Increased Activity

Rice is a model crop for studying host - pathogen interaction with one of the most devastating pathogens viz. Xanthomonas oryzae pv. oryzae (Xoo). In the present investigation, an attempt was made to isolate a virulent strain of Xathomonas oryzae from infected rice leaves and production of antioxidant enzymes, which are widely used in studying host - pathogen interactions. Among five isolates of X. oryzae pv. oryzae, SboBLB3 showed greater virulence as it showed susceptibility symptoms in infected rice leaves. The NCBI accession number of SboBLB3 was MH986180, which was obtained by sequencing 16s rDNA. The increased activity of antioxidant enzymes after SboBLB3 further confirms its virulence. Induction of antioxidant enzymes showed that SboBLB3 is a virulent strain of X. oryzae and can be used in host - pathogen interaction at molecular level.

scholarly journals Characterization of the role of COP9 signalosome in regulating cullin E3 ubiquitin ligase activity

2011 ◽  
Vol 22 (24) ◽  
pp. 4706-4715 ◽  
Author(s):  
Yin Yin Choo ◽  
Boon Kim Boh ◽  
Jessica Jie Wei Lou ◽  
Jolane Eng ◽  
Yee Chin Leck ◽  
...  
Keyword(s):  
Covalent Modification ◽  
Cop9 Signalosome ◽  
Major Mechanism ◽  
Ubiquitin Ligase Activity ◽  
Associated Proteins ◽  
Cullin Protein ◽  
Activation Cycle

Cullin RING ligases (CRLs) are the largest family of cellular E3 ubiquitin ligases and mediate polyubiquitination of a number of cellular substrates. CRLs are activated via the covalent modification of the cullin protein with the ubiquitin-like protein Nedd8. This results in a conformational change in the cullin carboxy terminus that facilitates the ubiquitin transfer onto the substrate. COP9 signalosome (CSN)-mediated cullin deneddylation is essential for CRL activity in vivo. However, the mechanism through which CSN promotes CRL activity in vivo is currently unclear. In this paper, we provide evidence that cullin deneddylation is not intrinsically coupled to substrate polyubiquitination as part of the CRL activation cycle. Furthermore, inhibiting substrate-receptor autoubiquitination is unlikely to account for the major mechanism through which CSN regulates CRL activity. CSN also did not affect recruitment of the substrate-receptor SPOP to Cul3, suggesting it may not function to facilitate the exchange of Cul3 substrate receptors. Our results indicate that CSN binds preferentially to CRLs in the neddylation-induced, active conformation. Binding of the CSN complex to active CRLs may recruit CSN-associated proteins important for CRL regulation. The deneddylating activity of CSN would subsequently promote its own dissociation to allow progression through the CRL activation cycle.

scholarly journals In vivo Host-Pathogen Interaction as Revealed by Global Proteomic Profiling of Zebrafish Larvae

2017 ◽  
Vol 7 ◽  
Author(s):  
Francisco Díaz-Pascual ◽  
Javiera Ortíz-Severín ◽  
Macarena A. Varas ◽  
Miguel L. Allende ◽  
Francisco P. Chávez
Keyword(s):  
Proteomic Profiling ◽  
Zebrafish Larvae ◽  
Host Pathogen Interaction ◽  
Host Pathogen
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