Identification of natural target proteins indicates functions of a serralysin -Type Metalloprotease, PrtA, in Anti-Immune Mechanisms

Gabriella Felföldi, Judit Marokházi, Miklós Képiró, I. Venekei

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Serralysins are generally thought to function as pathogenicity factors of bacteria, but so far no hard evidence of this (e.g., specific substrate proteins that are sensitive to the cleavage by these proteases) has been found. We have looked for substrate proteins to a serralysin-type proteinase, PrtA, in a natural host-pathogen molecular interaction system involving Manduca sexta and Photorhabdus luminescens. The exposure in vitro of hemolymph to PrtA digestion resulted in selective cleavage of 16 proteins, provisionally termed PAT (PrtA target) proteins. We could obtain sequence information for nine of these PrtA sensitive proteins, and by searching databases, we could identify six of them. Each has immune-related function involving every aspect of the immune defense: β-1,3 glucan recognition protein 2 (immune recognition), hemocyte aggregation inhibitor protein (HAIP), serine proteinase homolog 3, six serpin-1 variants, including serpin-1I (immune signaling and regulation), and scolexins A and B (coagulation cascade effector function). The functions of the identified PrtA substrate proteins shed new light on a possible participation of a serralysin in the virulence mechanism of a pathogen. Provided these proteins are targets of PrtA in vivo, this might represent, among others, a complex suppressive role on the innate immune response via interference with both the recognition and the elimination of the pathogen during the first, infective stage of the host-pathogen interaction. Our results also raise the possibility that the natural substrate proteins of serralysins of vertebrate pathogens might be found among the components of the innate immune system.

Original languageEnglish
Pages (from-to)3120-3126
Number of pages7
JournalApplied and Environmental Microbiology
Volume75
Issue number10
DOIs
Publication statusPublished - May 2009

Fingerprint

serralysin
metalloproteinases
protein
Proteins
proteins
pathogen
Serpins
Host-Pathogen Interactions
substrate
pathogens
cleavage
Peptide Hydrolases
Photorhabdus
proteinases
Myeloblastin
Photorhabdus luminescens
Manduca
PrtA metalloprotease
Hemocytes
host-pathogen interaction

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Food Science
  • Biotechnology
  • Ecology

Cite this

Identification of natural target proteins indicates functions of a serralysin -Type Metalloprotease, PrtA, in Anti-Immune Mechanisms. / Felföldi, Gabriella; Marokházi, Judit; Képiró, Miklós; Venekei, I.

In: Applied and Environmental Microbiology, Vol. 75, No. 10, 05.2009, p. 3120-3126.

Research output: Contribution to journalArticle

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