Differential Expression and Glycosylation of
            <i>Anaplasma phagocytophilum</i>
            Major Surface Protein 2 Paralogs during Cultivation in Sialyl Lewis x-Deficient Host Cells

Troese, Matthew J.; Sarkar, Manisha; Galloway, Nathan L.; Thomas, Russell J.; Kearns, Sarah A.; Reneer, Dexter V.; Yang, Tian; Carlyon, Jason A.

doi:10.1128/iai.01530-08

Cited by 13 publications

(9 citation statements)

References 49 publications

(69 reference statements)

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“…PSGL-1 CHO cells support A. phagocytophilum binding but not infection, while untransfected CHO cells lacking PSGL-1 expression do not support bacterial binding (5,70,78). A. phagocytophilum binding to PSGL-1 CHO cells occurs through bacterial engagement of sLe x -capped PSGL-1 and excludes interactions with other undefined receptors that facilitate PSGL-1/ sLe x -independent adherence (5,55,56,58,70,78). DC bacterial binding to PSGL-1 CHO cells did not increase ompA transcription (Fig.…”

Section: Resultsmentioning

confidence: 97%

“…Chinese hamster ovary cells transfected to express sLe x -capped PSGL-1 are ideal models for studying A. phagocytophilum interactions with PSGL-1 and sLe x (5,35,68,76,78). PSGL-1 CHO cells support A. phagocytophilum binding but not infection, while untransfected CHO cells lacking PSGL-1 expression do not support bacterial binding (5,70,78). A. phagocytophilum binding to PSGL-1 CHO cells occurs through bacterial engagement of sLe x -capped PSGL-1 and excludes interactions with other undefined receptors that facilitate PSGL-1/ sLe x -independent adherence (5,55,56,58,70,78).…”

Section: Resultsmentioning

confidence: 99%

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Anaplasma phagocytophilum Outer Membrane Protein A Interacts with Sialylated Glycoproteins To Promote Infection of Mammalian Host Cells

et al. 2012

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Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

Anaplasma phagocytophilum Outer Membrane Protein A Interacts with Sialylated Glycoproteins To Promote Infection of Mammalian Host Cells

et al. 2012

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“…PSGL-1 CHO cells (Chinese hamster ovary [CHO] cells transfected to express PSGL-1) are excellent models for studying A. phagocytophilum--PSGL-1 interactions (26,29,31,35,65,66). A. phagocytophilum binding to PSGL-1 CHO cells occurs exclusively through recognition of PSGL-1, and the bacterium cannot bind to untransfected CHO cells (31,35,67). DC binding to PSGL-1 CHO cells significantly upregulated asp14 transcription, with the most pronounced increase relative to carryover mRNA levels present in DC organisms occurring within the first hour (Fig.…”

Section: Resultsmentioning

confidence: 99%

Anaplasma phagocytophilum Asp14 Is an Invasin That Interacts with Mammalian Host Cells via Its C Terminus To Facilitate Infection

et al. 2013

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e Anaplasma phagocytophilum, a member of the family Anaplasmataceae, is the tick-transmitted obligate intracellular bacterium that causes human granulocytic anaplasmosis. The life cycle of A. phagocytophilum is biphasic, transitioning between the noninfectious reticulate cell (RC) and infectious dense-cored (DC) forms. We analyzed the bacterium's DC surface proteome by selective biotinylation of surface proteins, NeutrAvidin affinity purification, and mass spectrometry. Transcriptional profiling of selected outer membrane protein candidates over the course of infection revealed that aph_0248 (designated asp14 [14-kDa A. phagocytophilum surface protein]) expression was upregulated the most during A. phagocytophilum cellular invasion. asp14 transcription was induced during transmission feeding of A. phagocytophilum-infected ticks on mice and was upregulated when the bacterium engaged its receptor, P-selectin glycoprotein ligand 1. Asp14 localized to the A. phagocytophilum surface and was expressed during in vivo infection. Treating DC organisms with Asp14 antiserum or preincubating mammalian host cells with glutathione S-transferase (GST)-Asp14 significantly inhibited infection of host cells. Moreover, preincubating host cells with GST-tagged forms of both Asp14 and outer membrane protein A, another A. phagocytophilum invasin, pronouncedly reduced infection relative to treatment with either protein alone. The Asp14 domain that is sufficient for cellular adherence and invasion lies within the C-terminal 12 to 24 amino acids and is conserved among other Anaplasma and Ehrlichia species. These results identify Asp14 as an A. phagocytophilum surface protein that is critical for infection, delineate its invasion domain, and demonstrate the potential of targeting Asp14 in concert with OmpA for protecting against infection by A. phagocytophilum and other Anaplasmataceae pathogens.

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“…6B). Multiple isoforms of HusA may reflect the consequence of glycosylation or other posttranslational modifications to the expressed protein (37).…”

Section: Figure 6 Subcellular Localization and Detection Of Husa Isomentioning

confidence: 99%

Characterization of a Hemophore-like Protein from Porphyromonas gingivalis

Gao

Nguyen

Hunter

2010

Journal of Biological Chemistry

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The porphyrin auxotrophic pathogen Porphyromonas gingivalis obtains the majority of essential iron and porphyrin from host hemoproteins. To achieve this, the organism expresses outer membrane gingipains containing cysteine proteinase domains linked to hemagglutinin domains. Heme mobilized in this way is taken up by P. gingivalis through a variety of potential portals where HmuY/HmuR of the hmu locus are best described. These receptors have relatively low binding affinities for heme. In this report, we describe a novel P. gingivalis protein, HusA, the product of PG2227, which rapidly bound heme with a high binding constant at equilibrium of 7 ؋ 10 ؊10 M. HusA is both expressed on the outer membrane and released from the organism. Spectral analysis indicated an unusual pattern of binding where heme was ligated preferentially as a dimer. Further, the presence of dimeric heme induced protein dimer formation. Deletional inactivation of husA showed that expression of this moiety was essential for growth of P. gingivalis under conditions of heme limitation. This finding was in accord with the pronounced increase in gene expression levels for husA with progressive reduction of heme supplementation. Antibodies reactive against HusA were detected in patients with chronic periodontitis, suggesting that the protein is expressed during the course of infection by P. gingivalis. It is predicted that HusA efficiently sequesters heme from gingipains and fulfills the function of a high affinity hemophorelike protein to meet the heme requirement for growth of P. gingivalis during establishment of infection.

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Differential Expression and Glycosylation of Anaplasma phagocytophilum Major Surface Protein 2 Paralogs during Cultivation in Sialyl Lewis x-Deficient Host Cells

Cited by 13 publications

References 49 publications

Anaplasma phagocytophilum Outer Membrane Protein A Interacts with Sialylated Glycoproteins To Promote Infection of Mammalian Host Cells

Anaplasma phagocytophilum Outer Membrane Protein A Interacts with Sialylated Glycoproteins To Promote Infection of Mammalian Host Cells

Anaplasma phagocytophilum Asp14 Is an Invasin That Interacts with Mammalian Host Cells via Its C Terminus To Facilitate Infection

Characterization of a Hemophore-like Protein from Porphyromonas gingivalis

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