Serological Reactions of
            <i>Mycoplasma hominis</i>
            : Differences Among Mycoplasmacidal, Metabolic Inhibition, and Growth Agglutination Tests

Lin, Juey-Shin L.; Kass, Edward H.

doi:10.1128/iai.10.3.535-540.1974

Cited by 36 publications

(13 citation statements)

References 5 publications

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“…Strains of Mycoplasma hominis isolated from various healthy tissues and from patients with clinically diverse diseases exhibit marked phenotypic and genotypic heterogeneity (2,5,34). Antigenic variability among strains has been demonstrated by using protein analysis, direct or indirect hemagglutination, complement-dependent mycoplasmicidal activity, metabolic inhibition, and growth inhibition procedures (2,19,22,31,32,34,39). Many attempts have been made to find common antigenic features, especially features related to pathogenicity, among the different strains of M. hominis.…”

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Monoclonal antibodies to surface antigens of a pathogenic Mycoplasma hominis strain

et al. 1991

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Three monoclonal antibodies (MAbs) were prepared against an arthritogenic strain of Mycoplasma hominis isolated from the joint aspirates of a patient with chronic septic arthritis. Immunoblots of polyacrylamide gel-electrophoresed proteins before and after surface proteolysis showed that the predominant antigenic determinants were on surface-exposed polypeptides. These polypeptides have extensive hydrophobic characteristics, as demonstrated by Triton X-114 phase partitioning. The electrophoresed proteins from cells grown in medium containing [14C]palmitate were blotted onto nitrocellulose which was both reacted with the MAbs and exposed to X-ray film. Superimposable bands on both the immunoblots and the exposed film suggested that the proteins might be acylated. The MAbs were further tested for reactivity with 16 other strains of M. hominis isolated from patients with septic arthritis (1 strain), septicemia (10 strains), or nongonococcal urethritis (1 strain); from the cervix (1 strain), rectum (1 strain), or surgical wound (1 strain) of patients; and from a contaminated cell culture. No single protein was consistently recognized from strain to strain, although a 94-kDa protein from 16 of the 17 strains tested was bound by at least one of the MAbs. The apparent antigenic heterogeneity among strains of M. hominis, including those isolated from the same tissue source and/or from patients with the same type of clinical disease, might be misleading in that all strains express epitopes associated with a discrete number of proteins to which one, two, or all three MAbs bind. The expression of the epitopes on multiple proteins from the same or different strains may reflect a mechanism for generating antigenic diversity.

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Monoclonal antibodies to surface antigens of a pathogenic Mycoplasma hominis strain

et al. 1991

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“…Heterogeneities of the species of M. hominis were observed by serological methods (7,9,10), DNA-DNA hybridization (4), SDS-PAGE patterns (1,13), and restriction fragment length polymorphism (PFLP) using gene probes (3,5). Serological heterogeneity among M. hominis strains have been demonstrated by several serological methods (7,9,10), and Lin and Kass (9) proposed a subdivision of the species into seven serovars. Genomic homology of DNAs from 14 strains of M. hominis analyzed by DNA-DNA hybridization was in the range of 51 to 91% (4), and electrophoretic analysis of protein bands from the same 14 strains by SDS-PAGE showed 76 to 99% identity (1).…”

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Characterization of a Strain of Mycoplasma hominis Lacking 120 kDa Membrane Protein Isolated from Vero Cell Culture

Sasaki

Oyama³

et al. 1989

Microbiology and Immunology

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A strain of Mycoplasma hominis lacking a major membrane protein of 120 kDa was isolated from a Vero cell culture. This strain showed very slow growth rate and formed nipple-less colonies on agar medium.Strains of Mycoplasma hominis have been frequently isolated from various sites in humans, especially from the urogenital tracts (6,15,16), and from cell cultures (2, 11). In general, they require 2 to 3 culture days to reach maximum numbers of the viable organisms in liquid medium, and form fried-egg-like colonies on agar medium. A mycoplasma strain, H-4, was isolated as a contaminant of a Vero cell culture, and was identified as a strain of M. hominis by metabolism inhibition and growth inhibition tests. It grew very slowly compared with those of PG21 (the type strain) and two other clinical isolates of M. hominis and formed nipple-less colonies on agar medium. Then we compared the protein profiles of the cell membrane of the strain H-4 with other M. hominis strains including the type strain for the species.As the strain H-4 metabolized arginine, using eight antisera for arginineutilizing Mycoplasma species which are frequently isolated from cell cultures (2, 11), the metabolism inhibition and growth inhibition tests were performed (Table 1). Among eight antisera, only anti-M. hominis PG21 serum inhibited the metabolism and growth of the strain H-4; therefore, the strain H-4 was identified as M. hominis. The strain H-4 showed a similar extent of the growth under both aerobic and anaerobic conditions, but no improvement of the growth rate by the supplement of yeast extract into media. It showed no hemadsorption, and was sensitive to digitonin like other strains of M. hominis.These findings served to confirm the identification of the strain H-4. However, the strain H-4 required 6 to 7 culture days to reach maximum growth in liquid medium (Fig. 1), and formed nipple-less colonies on agar medium (Fig. 2). These characters of the H-4 did not change even after 15 passages.Four strains of M. hominis were used in cell protein analyses : the strain H-4, the type strain PG21, and two clinical isolates which were referred to as Miya-1 423

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“…The M. hominis strains selected for this study are shown in Table 1[10–15]. The strains are isolated from a wide variety of geographical and different anatomical sites.…”

Section: Methodsmentioning

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Cloning, sequencing and variability analysis of thegapgene fromMycoplasma hominis

Mygind

Søgaard

Melkova

et al. 2000

FEMS Microbiology Letters

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The gap gene encodes the glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The gene was cloned and sequenced from the Mycoplasma hominis type strain PG21(T). The intraspecies variability was investigated by inspection of restriction fragment length polymorphism (RFLP) patterns after polymerase chain reaction (PCR) amplification of the gap gene from 15 strains and furthermore by sequencing of part of the gene in eight strains. The M. hominis gap gene was found to vary more than the Escherichia coli counterpart, but the variation at nucleotide level gave rise to only a few amino acid substitutions. To verify that the gene was expressed in M. hominis, a polyclonal antibody was produced and tested against whole cell protein from 15 strains. The enzyme was expressed in all strains investigated as a 36-kDa protein. All strains except type strain PG21(T) showed reaction to a 104-kDa band in addition to the expected 36-kDa band. The protein reacting at 104 kDa is a M. hominis protein with either an epitope similar to one on GAPDH, or it is an immunoglobulin binding protein.

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Serological Reactions of Mycoplasma hominis : Differences Among Mycoplasmacidal, Metabolic Inhibition, and Growth Agglutination Tests

Cited by 36 publications

References 5 publications

Monoclonal antibodies to surface antigens of a pathogenic Mycoplasma hominis strain

Monoclonal antibodies to surface antigens of a pathogenic Mycoplasma hominis strain

Characterization of a Strain of Mycoplasma hominis Lacking 120 kDa Membrane Protein Isolated from Vero Cell Culture

Cloning, sequencing and variability analysis of thegapgene fromMycoplasma hominis

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