Matrix Metalloproteinases in Parasitic Infections

Bruschi, Fabrizio; Pinto, Barbara

doi:10.1007/978-981-10-6141-7_14

Cited by 3 publications

(5 citation statements)

References 154 publications

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“…The deduced NtMMP-9 had the typical structural characteristics of MMP family members, including the N-terminal signal peptide (1-21 aa), propeptide domain (38-96 aa), ZnMc domain (114-446 aa), and hemopexin-like repeats (HX domain) (494-674 aa), as well as a low complexity region (450-485 aa). The highly conserved sequence PRCGVPD was found in NtMMP-9 ( Figure 1), which agrees with the PRCXXPD motif (where X represents any aa) in MMPs [1]. This motif is regarded as a cysteine switch at the terminal of propeptide, and the cysteine switch is capable of coordinating the interaction between zinc atoms and cysteine thiolate via relieving chelation to regulate the zymogen form of MMPs [28].…”

Section: Cloning and Characterization Of Ntmmp-9supporting

confidence: 69%

“…The ZnMc domain consists of a conserved motif (HEFGHALGLDH, 402-412 aa) and three repeats of fibronectin type-II (FN2) domain ( Figure 1). This motif is the catalytic domain of MMP-9s, similar to the conserved zinc-binding motif (HEXXHXXGXXH, where X represents any aa) of MMPs [1,2]. The zinc-binding motif chelates the active site of Zn 2+ through three histidine residues [2].…”

Section: Cloning and Characterization Of Ntmmp-9mentioning

confidence: 99%

“…Matrix metalloproteinases (MMPs) are a family of 28 zinc-dependent endopeptidases [1], and they are widely distributed in all kingdoms of life [2]. MMPs are secreted as a form of zymogens, and can be activated through the conformational change or cysteine-switch proteolysis [3], which contributes to cleave an extracellular matrix (ECM) and to regulate pathological processes such as inflammation and innate immune defense [4,5] by degradation of the ECM, alteration of cell-cell and cell-ECM interactions, and cleavage of membrane proteins of cell surface and cleavage of proteins in the extracellular environment.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of Matrix Metalloprotease-9 Gene from Nile tilapia (Oreochromis niloticus) and Its High-Level Expression Induced by the Streptococcus agalactiae Challenge

et al. 2020

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The bacterial diseases of tilapia caused by Streptococcus agalactiae have resulted in the high mortality and huge economic loss in the tilapia industry. Matrix metalloproteinase-9 (MMP-9) may play an important role in fighting infection. However, the role of MMP-9 in Nile tilapia against S. agalactiae is still unclear. In this work, MMP-9 cDNA of Nile tilapia (NtMMP-9) has been cloned and characterized. NtMMP-9 has 2043 bp and encodes a putative protein of 680 amino acids. NtMMP-9 contains the conserved domains interacting with decorin and inhibitors via binding forces compared to those in other teleosts. Quantitative real-time-polymerase chain reaction (qPCR) analysis reveals that NtMMP-9 distinctly upregulated following S. agalactiae infection in a tissue- and time-dependent response pattern, and the tissues, including liver, spleen, and intestines, are the major organs against a S. agalactiae infection. Besides, the proteolytic activity of NtMMP-9 is also confirmed by heterologous expression and zymography, which proves the active function of NtMMP-9 interacting with other factors. The findings indicate that NtMMP-9 was involved in immune responses against the bacterial challenge at the transcriptional level. Further work will focus on the molecular mechanisms of NtMMP-9 to respond and modulate the signaling pathways in Nile tilapia against S. agalactiae invasion and the development of NtMMP-9-related predictive biomarkers or vaccines for preventing bacterial infection in the tilapia industry.

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Section: Cloning and Characterization Of Ntmmp-9supporting

confidence: 69%

Section: Cloning and Characterization Of Ntmmp-9mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization of Matrix Metalloprotease-9 Gene from Nile tilapia (Oreochromis niloticus) and Its High-Level Expression Induced by the Streptococcus agalactiae Challenge

et al. 2020

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“…In particular, metallopeptidases are a group of peptidases that are involved in the invasion of the host tissue by the parasite as they are able to degrade the extracellular matrix. In some cases, it has been suggested that the metallopeptidases conserve their proteolytic activity even after the antibody action exhibited by the host during infection by the parasite [4,5,18].…”

Section: Discussionmentioning

confidence: 99%

A novel nuclear marker and development of an ARMS-PCR assay targeting the metallopeptidase 10 (nas 10) locus to identify the species of theAnisakis simplex(s. l.) complex (Nematoda, Anisakidae)

et al. 2020

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The genus Anisakis represents one of the most widespread groups of ascaridoid nematodes in the marine ecosystem. Three closely related taxa are recognized in the Anisakis simplex (s. l.) complex: A. pegreffii, A. simplex (s. s.) and A. berlandi. They are widely distributed in populations of their intermediate/paratenic hosts (fish and squids) and definitive hosts (cetaceans). A novel nuclear gene locus, metallopeptidase 10 (nas 10) (451 bp), was sequenced and validated on a total of 219 specimens of the three species of Anisakis, collected in fish and cetacean hosts from allopatric areas included in their ranges of distribution. The specimens of Anisakis were first identified by allozymes and sequence analysis of the mtDNA cox2 and EF1α-1 nDNA. The novel nuclear marker has shown fixed alternative nucleotide positions in the three species, i.e. diagnostic at 100%, permitting the species determination of a large number of specimens analyzed in the present study. In addition, primers to be used for amplification-refractory mutation system (ARMS) PCR of the same gene locus were designed at these nucleotide positions. Thus, direct genotyping determination, by double ARMS, was developed and validated on 219 specimens belonging to the three species. Complete concordance was observed between the tetra-primer ARMS-PCR assays and direct sequencing results obtained for the nas 10 gene locus. The novel nuclear diagnostic marker will be useful in future studies on a multi-locus genotyping approach and also to study possible hybridization and/or introgression events occurring between the three species in sympatric areas.

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“…The metallopeptidases family is involved in the host tissue invasion by degrading the extracellular matrix. It has been also suggested that they conserve their proteolytic activity even after the action of the host antibodies [78,79]. Kim et al [21] found that some metallopeptidases genes are differentially regulated in the A. simplex (s.l.)…”

Section: Discussionmentioning

confidence: 99%

Differences in Gene Expression Profiles of Seven Target Proteins in Third-Stage Larvae of Anisakis simplex (Sensu Stricto) by Sites of Infection in Blue Whiting (Micromesistius poutassou)

Palomba

Cipriani

Giulietti

et al. 2020

Genes

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The third-stage larvae of the parasitic nematode genus Anisakis tend to encapsulate in different tissues including the musculature of fish. Host tissue penetration and degradation involve both mechanic processes and the production of proteins encoded by an array of genes. Investigating larval gene profiles during the fish infection has relevance in understanding biological traits in the parasite’s adaptive ability to cope with the fish hosts’ defense responses. The present study aimed to investigate the gene expression levels of some proteins in L3 of A. simplex (s.s.) infecting different tissues of blue whiting Micromesistius poutassou, a common fish host of the parasite in the NE Atlantic. The following genes encoding for Anisakis spp. proteins were studied: Kunitz-type trypsin inhibitor (TI), hemoglobin (hb), glycoprotein (GP), trehalase (treh), zinc metallopeptidase 13 (nas 13), ubiquitin-protein ligase (hyd) and sideroflexin 2 (sfxn 2). Significant differences in gene transcripts (by quantitative real-time PCR, qPCR) were observed in larvae located in various tissues of the fish host, with respect to the control. ANOVA analysis showed that relative gene expression levels of the seven target genes in the larvae are linked to the infection site in the fish host. Genes encoding some of the target proteins seem to be involved in the host tissue migration and survival of the parasite in the hostile target tissues of the fish host.

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Matrix Metalloproteinases in Parasitic Infections

Cited by 3 publications

References 154 publications

Characterization of Matrix Metalloprotease-9 Gene from Nile tilapia (Oreochromis niloticus) and Its High-Level Expression Induced by the Streptococcus agalactiae Challenge

Characterization of Matrix Metalloprotease-9 Gene from Nile tilapia (Oreochromis niloticus) and Its High-Level Expression Induced by the Streptococcus agalactiae Challenge

A novel nuclear marker and development of an ARMS-PCR assay targeting the metallopeptidase 10 (nas 10) locus to identify the species of theAnisakis simplex(s. l.) complex (Nematoda, Anisakidae)

Differences in Gene Expression Profiles of Seven Target Proteins in Third-Stage Larvae of Anisakis simplex (Sensu Stricto) by Sites of Infection in Blue Whiting (Micromesistius poutassou)

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