A mycoplasma high-affinity transport system and the in vitro invasiveness of mouse sarcoma cells.

Dudler, Robert; Schmidhauser, Christian; Parish, Roger W.; Wettenhall, Richard E.H.; Schmidt, Thomas

doi:10.1002/j.1460-2075.1988.tb03283.x

Cited by 118 publications

(107 citation statements)

References 38 publications

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“…A signal peptide, 23 amino acids in length, is present at the N-terminal of p37. These amino acids direct p37 to the cell outer membrane of M. hyorhinis [4] and p37 is exposed to host proteins when the bacterium infects eukaryotic cells. The signal peptide may guide the exportation of p37 protein from the host eukaryotic cells.…”

Section: Discussionmentioning

confidence: 99%

“…p37, a part of homologous high-affinity transport system in Mycoplasma hyorhinis [4,11], is known to enhance the invasiveness of melanoma (C8161 and A375M) and prostate carcinoma (PC-3 and Du-145) [6,12]. The colony-forming abilities of AGS and HEK 293T cells are greatly improved by p37 (unpublished data); however, the precise mechanism is still unknown.…”

Section: Introductionmentioning

confidence: 99%

“…Mycoplasma has been associated with many human diseases, such as pneumonitis and urinogenital infections [1][2][3]. Association between mycoplasma, carcinogenesis and metastasis has generally been supported although the underlying mechanism(s) remain an enigma [4][5][6][7][8]. Infectionrelated carcinogenesis, however, has been clearly documented with Helicobacter pylori, bacterium known to induce gastric cancer [9][10].…”

Section: Introductionmentioning

confidence: 99%

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Lipoprotein p37 from Mycoplasma hyorhinis inhibiting mammalian cell adhesion

et al. 2005

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Summaryp37 protein is a membrane lipoprotein of Mycoplasma hyorhinis, and our previous work showed that there was high ratio of M. hyorhinis infection in human gastric carcinoma. To investigate the possible functions of p37 in cancer development, the nucleotide sequence of p37 gene was modified and expressed well in transfected cells. We found that p37 localized at the Golgi apparatus and could be secreted out of the cell. Human gastric cancer cells AGS, after being transfected with the p37 gene, were smaller, more spherical and easy to detach from each other. Their adhesion to matrix was also diminished and cytoskeleton in these stable p37 AGS cell was rearranged and transcription co-factor b-actin was transferred to nucleolus with down-regulation of ICAM-1 and integrin b1. These findings will be helpful for us to elucidate the effects of p37 on eukaryotic cells as well as to better understand the potential relationship between cancer and mycoplasma infection.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Lipoprotein p37 from Mycoplasma hyorhinis inhibiting mammalian cell adhesion

et al. 2005

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“…Exact match primers specific for sequence positions 2071-2090 and 2403-2422, and sequence positions 2972-2991 and 3431-3450 as described in Ref. 9, were used to target p29 and p69 open reading frames using an annealing temperature of 50 C.…”

Section: Methodsmentioning

confidence: 99%

“…The fact that these peculiarities of the nucleotide sequence are characteristic of mycoplasmal gene sequences (10) led us to investigate the possibility that p40 represents a contaminating mycoplasmal protein. A literature search revealed that p40 is virtually identical to p37, which is one component of an operon determining a mycoplasmal membrane transport system for Mycoplasma hyorhinis (9).…”

Section: Methodsmentioning

confidence: 99%

Identification of a Human Cancer Related Organ‐Specific Neoantigen

Ilantzis

Thomson

Michaelidou

et al. 1993

Microbiology and Immunology

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: Human cancers express organ-specific neoaptigens (OSNs) which elicit specific cellular immune responses in the cancer patient, as demonstrated by leukocyte adherence inhibition (LAI), an in vitro immune response assay. A purified protein of MW 40,000 (p40) exhibiting OSN (colon specific) activity was cleaved into specific peptide fragments and their partial amino acid sequences determined. This information was used in the polymerase chain reaction (PCR) to obtain a 992 by cDNA clone (PCR-992) from a human colon adenocarcinoma cell line (LS-180). By comparison of the predicted amino acid sequence of PCR-992 with the known sequence of p40 peptides, PCR-992 was shown to correspond to almost the entire coding region of p40. Nucleotide sequence analysis suggested that the protein was mycoplasmal in origin due to its high A H-T content (76%) and the presence of five in frame TGA termination codons ; at least two of the latter are actually read as tryptophan, a known feature of mycoplasma translation. We have confirmed this origin by direct isolation of a contaminating mycoplasma species from the LS-180 cell line and demonstration that it could be hybridized with the PCR-992 probe. Northern and PCR analysis of RNA preparations from the contaminated LS-180 cell line showed that p40 was part of the high affinity transport system operon of Mycoplasma hyorhinis (Dudler et al, EMBO J., 7: 3963-3970, 1988). Total protein lysates of Mycoplasma hyorhinis cultivated without animal cells could elicit positive LAI responses when incubated with cancer patient leukocytes but not with normal patient leukocytes. The organ-specific nature of the response was, however, not observed indicating that host cell-mycoplasmal interactions may play a role in determining the organspecific nature of p40 seen with the LAI. The significance of these findings will be discussed in the context of previous thinking regarding the origin of OSNs.

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