Expression of LAP, a SecA2-dependent secretory protein, is induced under anaerobic environment

Burkholder, Kristin M.; Kim, Kwang Pyo; Mishra, K. K.; Medina, Sarimar; Hahm, Byoung-Kwon; Kim, Hyochin; Bhunia, Arun K.

doi:10.1016/j.micinf.2009.05.006

Cited by 74 publications

(127 citation statements)

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“…49 The auxiliary protein secretion system (SecA2) of L. monocytogenes was shown to be involved in the secretion of several virulence factors involved in different steps of the infectious process (LAP, FbpA, p60, OppA, MurA and Sod). 33,46,206,207 In accordance, SecA2 expression promotes bacterial adhesion and invasion, intracellular multiplication and cell-cell spread and is required for virulence in mice. In addition, SecA2-secreted mutants lacking a functional PrfA are unable to grow in infected cells and are 100,000-fold less virulent in mice than wild-type strains.…”

Section: O N O T D I S T R I B U T Ementioning

confidence: 97%

“…Oral administration of lap-deficient strains to mice confirmed that Lap is essential for full virulence. 33 Ami is a 99 kDa protein exhibiting N-acetylmuramoyl-Lalanine amidase activity. 34 Its N-terminal domain is responsible for cleavage of the amide bond between N-acetylmuramic acid and l-alanine residues in the peptidoglycan.…”

Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

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The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

et al. 2011

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Section: O N O T D I S T R I B U T Ementioning

confidence: 97%

Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

et al. 2011

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“…To determine if secreted LAP is able to reassociate on the surface of L. innocua cells, we exposed this bacterium to a LAP preparation from L. monocytogenes and examined adhesion to Caco-2 cells as described before (Burkholder et al, 2009). Briefly, LAP was prepared from stationary-phase culture supernatant of L. monocytogenes F4244 and filtered (0.22 mm).…”

Section: Analysis Of the Surface Expression Of Lap On Listeria Cellsmentioning

confidence: 99%

“…Previous research has demonstrated that LAP interacts with the cellular receptor Hsp60 (Wampler et al, 2004), and exhibits preferential affinity towards cells of intestinal origin Kim et al, 2006;Pandiripally et al, 1999). We have recently shown that LAP secretion is essential for L. monocytogenes pathogenesis and that its secretion is SecA2-dependent (Burkholder et al, 2009). The L. monocytogenes lap (lmo1634) gene was identified as encoding an alcohol acetaldehyde dehydrogenase, a housekeeping enzyme (Kim, 2004).…”

Section: Introductionmentioning

confidence: 98%

“…In Mycobacterium tuberculosis, the reassociation of the housekeeping enzyme malate synthase on the surface allows bacteria to adhere to host laminin and fibronectin during infection (Kinhikar et al, 2006). Similarly, secreted LAP has been shown to reassociate on the surface of L. monocytogenes cells prior to binding to mammalian cells (Burkholder et al, 2009). Although housekeeping enzymes of many pathogens act as virulence factors, often by secretion and reassociation on their surfaces, the role of these virulence factors in non-pathogenic species of the same genera is unknown.…”

Section: Introductionmentioning

confidence: 99%

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LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species

et al. 2010

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Listeria adhesion protein (LAP), an alcohol acetaldehyde dehydrogenase (lmo1634), interacts with host-cell receptor Hsp60 to promote bacterial adhesion during the intestinal phase of Listeria monocytogenes infection. The LAP homologue is present in pathogens (L. monocytogenes, L. ivanovii) and non-pathogens (L. innocua, L. welshimeri, L. seeligeri); however, its role in nonpathogens is unknown. Sequence analysis revealed 98 % amino acid similarity in LAP from all Listeria species. The N-terminus contains acetaldehyde dehydrogenase (ALDH) and the Cterminus an alcohol dehydrogenase (ADH). Recombinant LAP from L. monocytogenes, L. ivanovii, L. innocua and L. welshimeri exhibited ALDH and ADH activities, and displayed strong binding affinity (K D 2-31 nM) towards Hsp60. Flow cytometry, ELISA and immunoelectron microscopy revealed more surface-associated LAP in pathogens than non-pathogens. Pathogens exhibited significantly higher adhesion (P,0.05) to Caco-2 cells than non-pathogens; however, pretreatment of bacteria with Hsp60 caused 47-92 % reduction in adhesion only in pathogens. These data suggest that biochemical properties of LAP from pathogenic Listeria are similar to those of the protein from non-pathogens in many respects, such as substrate specificity, immunogenicity, and binding affinity to Hsp60. However, protein fractionation analysis of extracts from pathogenic and non-pathogenic Listeria species revealed that LAP was greatly reduced in intracellular and cell-surface protein fractions, and undetectable in the extracellular milieu of nonpathogens even though the lap transcript levels were similar for both. Furthermore, a LAP preparation from L. monocytogenes restored adhesion in a lap mutant (KB208) of L. monocytogenes but not in L. innocua, indicating possible lack of surface reassociation of LAP molecules in this bacterium. Taken together, these data suggest that LAP expression level, cellsurface localization, secretion and reassociation are responsible for LAP-mediated pathogenicity and possibly evolved to adapt to a parasitic life cycle in the host.

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SecA2 is not required for secretion of the surface autolysin IspC in Listeria monocytogenes serotype 4b

Ronholm

Zhang

Cao

et al. 2013

J. Basic Microbiol.

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Listeria monocytogenes is one of several Gram-positive bacteria known to contain an auxiliary ATPase (SecA2) involved in the Sec secretion of a subset of proteins important to bacterial pathogenesis, including autolysins. It is not known if IspC, a novel surface-associated autolysin essential for full virulence of L. monocytogenes serotype 4b, is SecA2-dependent for secretion. By creating a secA2 gene deletion (ΔsecA2) mutant from the wild type (WT) L. monocytogenes serotype 4b strain, in combination with the proteomic analysis of surface proteins and those secreted into the medium from both the mutant and the WT, we confirmed previous findings that two autolysins (p60 and NamA) are SecA2-dependent for secretion. However, this approach did not identify IspC as one of the surface proteins affected by the SecA2 deletion. Further experiments with immunofluorescence microscopy and Western blotting indicated that IspC was well displayed on the surface of both the ΔsecA2 mutant and WT cells, while p60 was not, clearly indicating that the secretion of IspC is not attributed to the SecA2 pathway. This finding sets IspC apart from other autolysins involved in virulence, such as p60 and NamA, in that SecA2 is not required for IspC secretion.

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Expression of LAP, a SecA2-dependent secretory protein, is induced under anaerobic environment

Cited by 74 publications

References 31 publications

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species

SecA2 is not required for secretion of the surface autolysin IspC in Listeria monocytogenes serotype 4b

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