Host-Pathogen Interactions

Southwood, Dean; Ranganathan, Shoba

doi:10.1016/b978-0-12-809633-8.20088-5

Cited by 9 publications

(7 citation statements)

References 90 publications

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“…Host-pathogen interactions (HPIs) are complex and dynamic in nature and crucial for our understanding of infectious diseases. Most studies on HPIs primarily focus on how pathogens attack and exploit hosts, e.g., how pathogen invades hosts, evades from host defense, and proliferates in hosts, and in turn how host protects themselves against pathogens, e.g., how host immune responds to invaders [52].…”

Section: Host-pathogen Interactionsmentioning

confidence: 99%

Role of Protein Glycosylation in Host-Pathogen Interaction

Lin

Xue

Liao

et al. 2020

Cells

127

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Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate protein conformation, activity, and stability, etc. This review summarizes various roles of different glycoproteins during the interaction, which include: host glycoproteins prevent pathogens as barriers; pathogen glycoproteins promote pathogens to attack host proteins as weapons; pathogens glycosylate proteins of the host to enhance virulence; and hosts sense pathogen glycoproteins to induce resistance. In addition, this review also intends to summarize the roles of lectin (a class of protein entangled with glycoprotein) in host-pathogen interactions, including bacterial adhesins, viral lectins or host lectins. Although these studies show the importance of protein glycosylation in host-pathogen interaction, much remains to be discovered about the interaction mechanism.

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Section: Host-pathogen Interactionsmentioning

confidence: 99%

Role of Protein Glycosylation in Host-Pathogen Interaction

Lin

Xue

Liao

et al. 2020

Cells

127

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“…A systems level understanding of interactions between pathogen and host proteins is a crucial step to establish a relationship between pathogen and host [ 24 ]. A collective study of interactions by multiple pathogens provides an insight about the mutual effect and strategy of pathogens to create the disease condition.…”

Section: Discussionmentioning

confidence: 99%

“…New proposed measures of centrality coined for HPIs to aid in the design of multipurpose drugs include Connectivity of human proteins targeted by same virus protein, propagation speed, diversity of predators, decreased shortest path, component index, crown centrality and vulnerable centrality [ 23 ]. The development of novel drugs, vaccines and other therapeutics for CVDs caused by microorganisms is highly dependent on the knowledge gained from investigating HPIs [ 24 ].…”

Section: Introductionmentioning

confidence: 99%

Network analysis of host-pathogen protein interactions in microbe induced cardiovascular diseases

Singh

Rai

Bhatnagar

et al. 2022

ISB

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Large-scale visualization and analysis of HPIs involved in microbial CVDs can provide crucial insights into the mechanisms of pathogenicity. The comparison of CVD associated HPIs with the entire set of HPIs can identify the pathways specific to CVDs. Therefore, topological properties of HPI networks in CVDs and all pathogens was studied using Cytoscape3.5.1. Ontology and pathway analysis were done using KOBAS 3.0. HPIs of Papilloma, Herpes, Influenza A virus as well as Yersinia pestis and Bacillus anthracis among bacteria were predominant in the whole (wHPI) and the CVD specific (cHPI) network. The central viral and secretory bacterial proteins were predicted virulent. The central viral proteins had higher number of interactions with host proteins in comparison with bacteria. Major fraction of central and essential host proteins interacts with central viral proteins. Alpha-synuclein, Ubiquitin ribosomal proteins, TATA-box-binding protein, and Polyubiquitin-C &B proteins were the top interacting proteins specific to CVDs. Signaling by NGF, Fc epsilon receptor, EGFR and ubiquitin mediated proteolysis were among the top enriched CVD specific pathways. DEXDc and HELICc were enriched host mimicry domains that may help in hijacking of cellular machinery by pathogens. This study provides a system level understanding of cardiac damage in microbe induced CVDs.

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“…In nature, host–pathogen Protein–protein interactions (HP-PPIs) are ubiquitous and essential for initiation and propagation of infectious diseases (Dean Southwood 2019 ). Pathogenesis involves interactions between the signalling networks of the host and pathogen.…”

Section: Introductionmentioning

confidence: 99%

ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions

et al. 2022

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Molecular mimicry of host proteins by pathogens constitutes a strategy to hijack the host pathways. At present, there is no dedicated resource for mimicked domains and motifs in the host–pathogen interactome. In this work, the experimental host–pathogen (HP) and host–host (HH) protein–protein interactions (PPIs) were collated. The domains and motifs of these proteins were annotated using CD Search and ScanProsite, respectively. Host and pathogen proteins with a shared host interactor and similar domain/motif constitute a mimicry pair exhibiting global structural similarity (domain mimicry pair; DMP) or local sequence motif similarity (motif mimicry pair; MMP). Mimicry pairs are likely to be co-expressed and co-localized. 1,97,607 DMPs and 32,67,568 MMPs were identified in 49,265 experimental HP-PPIs and organized in a web-based resource, ImitateDB ( http://imitatedb.sblab-nsit.net ) that can be easily queried. The results are externally integrated using hyperlinked domain PSSM ID, motif ID, protein ID and PubMed ID. Kinase, UL36, Smc and DEXDc were frequent DMP domains whereas protein kinase C phosphorylation, casein kinase 2 phosphorylation, glycosylation and myristoylation sites were frequent MMP motifs. Novel DMP domains SANT, Tudor, PhoX and MMP motif microbody C-terminal targeting signal, cornichon signature and lipocalin signature were proposed. ImitateDB is a novel resource for identifying mimicry in interacting host and pathogen proteins. Supplementary Information The online version contains supplementary material available at 10.1007/s00726-022-03163-3.

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Host-Pathogen Interactions

Cited by 9 publications

References 90 publications

Role of Protein Glycosylation in Host-Pathogen Interaction

Role of Protein Glycosylation in Host-Pathogen Interaction

Network analysis of host-pathogen protein interactions in microbe induced cardiovascular diseases

ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions

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