Tissue Distribution of the Pk Antigen as Determined by a Monoclonal Antibody

Kasai, Kiyoshi; Galton, Jane; Terasaki, Paul I.; Wakisaka, Akemi; Kawahara, Mutsuto; Root, Thomas; Hakomori, Sen‐itiroh

doi:10.1111/j.1744-313x.1985.tb00848.x

Cited by 39 publications

(15 citation statements)

References 9 publications

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“…Gb3 is the pK blood group antigen (34). Tissue surveys using anti-PK antisera have shown that human ovaries do not express this glycolipid (35). Our data are consistent with this finding: low levels of Gb3 were detected in some "normal" ovarian tissue, but the levels were markedly elevated in the ovarian tumor tissue samples.…”

Section: Methodssupporting

confidence: 81%

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1.

Farkas-Himsley

Hill

Rosen

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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We have identified verotoxin 1 (VT1) as the active component within an antineoplastic bacteriocin preparation from Escherichia coli HSC10 studied over two decades. Recombinant VT1 can simulate the toxicity of anticancer proteins (ACP), and the antineoplastic activity of ACP (and VT1) was abrogated by treatment with anti-VTI antibody. Similarly, VT1 mimics the protective effect ofACP in a murine metastatic fibrosarcoma model. Prior immunization with VT1 B subunit prevents the effect ofVT1 or ACP in this model. The activity of ACP against a variety of human ovarian cell lines was mimicked by VT1, and multidrug-resistant variants were significantly hypersensitive. Primary ovarian tumors and metastases contain elevated levels of globotriaosylceramide compared with normal ovaries, and overlay of frozen tumor sections showed selective VT binding to tumor tissue and the lumen of invading blood vessels. Our contention that VT1 could provide an additional approach to the management of certain human neoplasms is discussed.Bacteriocins are bacterial proteins produced to prevent the growth of competing microorganisms in a particular biological niche. A preparation of bacteriocin from a strain ofEscherichia coli (HSC1o) has long been shown to have antineoplastic activity against a variety of human tumor cell lines in vitro (1-3) and more recently against Mycosis fungoides skin tumors in man (R. Schachter, personal communication). This preparation of partially purified bacteriocin (PPB) or anticancer proteins (ACP) (3) was also effective in a murine sarcoma tumor model to prevent metastases to the lung from an intravenous injection (3).We now demonstrate that verotoxin 1 (VT1) is the active component within the ACP preparation and that purified VT1 has a potent antineoplastic effect in vitro and in vivo.

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Section: Methodssupporting

confidence: 81%

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1.

Farkas-Himsley

Hill

Rosen

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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“…This mutant was shown to display elevated sensitivity to serum-mediated killing. Further, the P k epitope is also present on the surface of erythrocytes and several epithelial cell types (79), and because of this immunochemical identity, no naturally occurring antibodies toward the P k epitope of M. catarrhalis LOS are likely to be present in human serum. Loss of the P k epitope then apparently results in the exposure of a different LOS epitope and, subsequently, to the activation of the complement system (156).…”

Section: Losmentioning

confidence: 99%

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Vries

Bootsma

Hays

et al. 2009

Microbiol Mol Biol Rev

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SUMMARY In recent years, Moraxella catarrhalis has established its position as an important human mucosal pathogen, no longer being regarded as just a commensal bacterium. Further, current research in the field has led to a better understanding of the molecular mechanisms involved in M. catarrhalis pathogenesis, including mechanisms associated with cellular adherence, target cell invasion, modulation of the host's immune response, and metabolism. Additionally, in order to be successful in the host, M. catarrhalis has to be able to interact and compete with the commensal flora and overcome stressful environmental conditions, such as nutrient limitation. In this review, we provide a timely overview of the current understanding of the molecular mechanisms associated with M. catarrhalis virulence and pathogenesis.

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“…These data suggest that resistance to serum complement-mediated killing may be related to the presence of the two terminal galactose residues on the LOS. These residues form part of a structure that has been shown to be immunochemically identical to the P k (Gal␣1-4Gal␤1-4Glc) antigen found on a number of human cells including erythrocytes, as well as gastrointestinal, ureteral, and bladder epithelial cells (7,29,35). It would appear that the Moraxella Gal␣1-4Gal␤1-4Glc structure may act as a human self-antigen and that antibodies to it are not present in normal human serum.…”

Section: Discussionmentioning

confidence: 93%

Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Zaleski¹,

Scheffler

Densen

et al. 2000

Infect Immun

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Moraxella catarrhalis is a respiratory pathogen responsible for acute bacterial otitis media in children and exacerbation of chronic bronchitis in adults. M. catarrhalis strains are frequently resistant to the bactericidal activity of normal human serum. In order to determine if the lipooligosaccharide (LOS) of M. catarrhalis has a role in serum resistance, the UDP-glucose-4-epimerase (galE) gene was identified, cloned, and sequenced and a deletion/insertion mutation was introduced into M. catarrhalis strain 2951. GalE enzymatic activity, measured in whole-cell lysates, was ablated in M. catarrhalis 2951 galE. Mass spectrometric analysis of LOS isolated with hot phenol-water confirmed that strain 2951 produced a type A LOS. These studies showed that the LOS from 2951 galE had lost two hexose residues due to the galE mutation and that the resultant LOS structure lacked the (Gal␣1-4Gal␤1-4Glc) P k epitope found on M. catarrhalis 2951. Wild-type M. catarrhalis 2951 is resistant to complement-mediated serum bactericidal activity. In contrast, a greater than 2-log 10 -unit reduction in CFU occurred after incubation of 2951 galE in either 50 or 25% pooled human serum (PNHS), and CFU in 10% PNHS decreased by about 1 log 10 unit. These studies suggest that the P k epitope of the LOS may be an important factor in the resistance of M. catarrhalis to the complement-mediated bactericidal effect of normal human serum.Moraxella catarrhalis is a human respiratory pathogen that is currently the third leading cause of otitis media along with Streptococcus pneumoniae and Haemophilus influenzae (10). Studies from various centers in the United States, Europe, and Asia used tympanocentesis to demonstrate that 15 to 20% of the middle-ear infections occurring in young children were caused by M. catarrhalis (10,15,16,18,46). M. catarrhalis has also been implicated as an important cause of respiratory disease in adults with predisposing conditions (41). Studies from several centers have reported clusters of nosocomial outbreaks of M. catarrhalis, most of which occurred in pulmonary care units (43,45). Although multiple studies have described specific bacterial components considered potential virulence factors, the steps involved in the pathogenesis of M. catarrhalis colonization and infection remain elusive (28, 41). One feature of this organism which has stimulated the interest of a number of investigators is its resistance to killing by normal human serum. Recent studies have focused on components of the bacterial outer membrane, as these structures would most likely be available for interaction with the host immune response. One prominent bacterial surface component, implicated as a potential virulence factor, is the lipooligosaccharide (LOS).The LOS is similar to those of other airway pathogens such as H. influenzae, Neisseria meningitidis, and Bordetella pertussis in lacking O antigens typical of the enteric gram-negative bacilli. There are three M. catarrhalis serotypes (A, B, and C) based on chemically defined differences in the ...

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Tissue Distribution of the Pk Antigen as Determined by a Monoclonal Antibody

Cited by 39 publications

References 9 publications

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1.

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1.

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

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Tissue Distribution of the Pk Antigen as Determined by a Monoclonal Antibody

Cited by 39 publications

References 9 publications

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1.

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1.

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Lipooligosaccharide P k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

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Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum