Comparison of host responses after intranasal infection of guinea-pigs with Mycoplasma genitalium or with Mycoplasma pneumoniae

1991 ◽  
Vol 10 (3) ◽  
pp. 221-229 ◽  
Author(s):  
Enno Jacobs ◽  
Thomas Watter ◽  
Hans E. Schaefer ◽  
Wolfgang Bredt
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Guinea Pigs ◽  
Mycoplasma Genitalium ◽  
Host Responses ◽  
Intranasal Infection

scholarly journals Characterization of MGC2, a Mycoplasma gallisepticum Cytadhesin with Homology to the Mycoplasma pneumoniae 30-Kilodalton Protein P30 and Mycoplasma genitalium P32

1998 ◽  
Vol 66 (7) ◽  
pp. 3436-3442 ◽  
Author(s):  
Linda L. Hnatow ◽  
Calvin L. Keeler ◽  
Laura L. Tessmer ◽  
Kirk Czymmek ◽  
John E. Dohms
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Reverse Transcription ◽  
Mycoplasma Genitalium ◽  
Mycoplasma Gallisepticum ◽  
Immunogold Labeling ◽  
Respiratory Pathogen ◽  
Functional Studies ◽  
Reverse Transcription Pcr ◽  
Attachment Inhibition

ABSTRACT A second cytadhesin-like protein, MGC2, was identified in the avian respiratory pathogen Mycoplasma gallisepticum. The 912-nucleotide mgc2 gene encodes a 32.6-kDa protein with 40.9 and 31.4% identity with the M. pneumoniae P30 andM. genitalium P32 cytadhesins, respectively. Functional studies with reverse transcription-PCR, immunoblotting, double-sided immunogold labeling, and attachment inhibition assays demonstrated homology to the human mycoplasmal P30 and P32 cytadhesins. These findings suggest that there is a family of cytadhesin genes conserved among pathogenic mycoplasmas infecting widely divergent hosts.

scholarly journals Uncoupling of the apyrimidinic/apurinic endonucleolytic and 3′→5′ exonucleolytic activities of the Nfo protein of Mycoplasma pneumoniae through mutation of specific amino acid residues

Microbiology ◽  
2014 ◽  
Vol 160 (6) ◽  
pp. 1087-1100 ◽  
Author(s):  
Silvia Estevão ◽  
Pieternella E. van der Spek ◽  
Annemarie M. C. van Rossum ◽  
Cornelis Vink
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Divalent Cations ◽  
Single Point ◽  
Dna Recombination ◽  
Point Mutations ◽  
Mycoplasma Genitalium ◽  
Amino Acid Residues ◽  
Specific Amino Acid ◽  
Cleavage Activity ◽  
Ap Sites

The DNA recombination and repair machineries of Mycoplasma pneumoniae and Mycoplasma genitalium were predicted to consist of a set of ~11 proteins. The function of one of these proteins was inferred from its homology with proteins belonging to the Endo IV enzyme family. The members of this family function in the repair of apyrimidinic/apurinic (AP) sites in DNA. As such activity may be crucial in the mycoplasmal life cycle, we set out to study the Endo IV-like proteins encoded by M. pneumoniae and M. genitalium. Both proteins, termed Nfo Mpn and Nfo Mge , respectively, were assessed for their ability to interact with damaged and undamaged DNA. In the absence of divalent cations, both proteins exhibited specific cleavage of AP sites. Surprisingly, the proteins also recognized and cleaved cholesteryl-bound deoxyribose moieties in DNA, showing that these Nfo proteins may also function in repair of large DNA adducts. In the presence of Mg2+, Nfo Mpn and Nfo Mge also showed 3′→5′ exonucleolytic activity. By introduction of 13 single point mutations at highly conserved positions within Nfo Mpn , two major types of mutants could be distinguished: (i) mutants that showed no, or limited, AP cleavage activity in the presence of EDTA, but displayed significant levels of AP cleavage activity in the presence of Mg2+; these mutants displayed no, or very low, exonucleolytic activity; and (ii) mutants that only demonstrated marginal levels of AP site cleavage activity in the presence of Mg2+ and did not show exonucleolytic activity. Together, these results indicated that the AP endonucleolytic activity of the Nfo Mpn protein can be uncoupled from its 3′→5′ exonucleolytic activity.

scholarly journals In Vitro Activities of Eravacycline and Other Antimicrobial Agents against Human Mycoplasmas and Ureaplasmas

2020 ◽  
Vol 64 (8) ◽  
Author(s):  
Ken B. Waites ◽  
Donna M. Crabb ◽  
Li Xiao ◽  
Lynn B. Duffy ◽  
Sixto M. Leal
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Antimicrobial Agents ◽  
Susceptibility Testing ◽  
Ureaplasma Urealyticum ◽  
Mycoplasma Hominis ◽  
Mycoplasma Genitalium ◽  
Content Type ◽  
Ureaplasma Parvum

ABSTRACT We performed in vitro susceptibility testing for eravacycline in comparison to 4 other antimicrobials against 10 Mycoplasma genitalium, 40 Mycoplasma hominis, 44 Mycoplasma pneumoniae, 20 Ureaplasma parvum, and 20 Ureaplasma urealyticum isolates. All eravacycline MICs were ≤0.25 μg/ml, except that for one isolate of M. genitalium, for which the MIC was 2 μg/ml. Eravacycline was markedly more potent than tetracycline, azithromycin, moxifloxacin, and clindamycin against all isolates tested, which included 37 macrolide, tetracycline, and/or fluoroquinolone-resistant organisms.

scholarly journals Analysis of host responses of guinea pigs during Helicobacter pylori infection

2001 ◽  
Vol 30 (2) ◽  
pp. 151-156 ◽  
Author(s):  
S. G. Rijpkema ◽  
Z. Durrani ◽  
G. Beavan ◽  
J. R. Gibson ◽  
J. Luck ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Guinea Pigs ◽  
Helicobacter Pylori Infection ◽  
Host Responses

scholarly journals Comparative In Vitro Susceptibilities of Human Mycoplasmas and Ureaplasmas to a New Investigational Ketolide, CEM-101

2009 ◽  
Vol 53 (5) ◽  
pp. 2139-2141 ◽  
Author(s):  
Ken B. Waites ◽  
D. M. Crabb ◽  
Lynn B. Duffy
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Mycoplasma Hominis ◽  
Mycoplasma Genitalium ◽  
Mycoplasma Fermentans

ABSTRACT MICs were determined for an investigational ketolide, CEM-101, and azithromycin, telithromycin, doxycycline, levofloxacin, clindamycin, and linezolid against 36 Mycoplasma pneumoniae, 5 Mycoplasma genitalium, 13 Mycoplasma hominis, 15 Mycoplasma fermentans, and 20 Ureaplasma isolates. All isolates, including two macrolide-resistant M. pneumoniae isolates, were inhibited by CEM-101 at ≤0.5 μg/ml, making CEM-101 the most potent compound tested.

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