Two penicillin binding proteins of Haemophilus influenzae are lost after cells enter stationary phase

Mendelman, Paul L.

doi:10.1016/0378-1097(85)90348-9

Cited by 9 publications

(18 citation statements)

References 7 publications

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“…Furthermore, the PBP profile of the H . injluenzae type strain was identical to that of 10 other susceptible isolates previously described (Mendelman and Chaffin, 1985 ;Serfass et al 1986;Mendelman et al, 1987).…”

Section: Resultssupporting

confidence: 65%

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The penicillin binding proteins of the genus Haemophilus

Mendelman

Serfass

1988

Journal of Medical Microbiology

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Summary. We questioned whether the penicillin binding protein (PBP) profiles of representative strains from the 19 species varied within the genus Haernophilus and whether these profiles would be of taxonomic value. Seventeen of the 19 representative strains studied had distinct PBP profiles; only those of H . aviurn and H.paragal1inarurn were identical. The data support the inclusion of H . aegyptius in the genus as a species related to but separate from H . influenzae and could not exclude H . sornnus, H . agni, and H . equigenitalis from the genus. Comparative PBP analysis within the genus Haemophilus may therefore be useful taxonomically.

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Section: Resultssupporting

confidence: 65%

“…H. ducreyi was labelled after growth for 4 days. Electrophoresis and processing were performed as previously described (Mendelman and Chaffin, 1985); the autofluorograms were developed after exposure for 14 days.…”

Section: Methodsmentioning

confidence: 99%

The penicillin binding proteins of the genus Haemophilus

Mendelman

Serfass

1988

Journal of Medical Microbiology

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“…This is in contrast to the previous reports and suggests that P B P 4 may be subject to inter-strain variability independent of ampicillin resistance. The PBPs designated 3A and 3B (68 and 65 kDa, respectively) by Parr & Bryan (1984), and PBPs designated 4 and 5 (62 and 59 kDa, respectively) by Mendelman & Chaffin (1985) appear to correspond to our PBPs 4 and 5 (59 and 56 kDa, respectively). The differences in reported molecular mass presumably reflect minor differences in technique.…”

Section: A S E R F a S S A N D O T H E R Smentioning

confidence: 81%

“…infruenzae ATCC 19148 and to four additional ampicillin-susceptible isolates studied by Mendelman & Chaffin (1985). Eight PBPs were detected.…”

Section: A S E R F a S S A N D O T H E R Smentioning

confidence: 99%

“…Whether these additional PBPs are simply another example of inter-strain variability or are related to ampicillin resistance must be confirmed by isogenic comparisons. However, it is noteworthy that neither of' these two PBPs has been detected in the I0 susceptible strains for which PBP profiles have been examined and reported (Makover rt al., 198 1 ;Mendelman & Chaffin, 1985 ;Parr & Bryan, 1984). Since multiple alterations are very likely to involve several genetic steps, transformation studies could identify which PBPs change along with resistance.…”

Section: A S E R F a S S A N D O T H E R Smentioning

confidence: 99%

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Ampicillin Resistance and Penicillin-binding Proteins of Haemophilus influenzae

et al. 1986

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Penicillin-binding protein (PBP) alterations have been associated with non-p-lactamasemediated ampicillin resistance in Haemophilus injhenzae. We evaluated the PBP profiles of several ampicillin-susceptible and -resistant clinical isolates of H. injluenzae to determine how consistently the described alterations occurred, and to document the reproducibility of the PBP profiles for this species. The MIC of ampicillin ranged from 0.06 to 0.13 pg ml-I for the susceptible isolates at an inoculum of 100000 c.f.u. when tested by broth dilution, and was 0-5 pg.ml-I for all four isolates when tested by agar dilution. The MIC for the resistant isolates ranged from 4 to 8 pg mi-' when tested by broth dilution, and from 1.5 to 16 ug ml-1 when tested by agar dilution. At least eight distinct PBPs with molecular masses ranging from 27 to 90 kDa were detected both in cell membrane preparations and whole cell (in oivo) binding assays done on cells in the exponential growth phase. PBP variability was evident both in the ampicillinsusceptible and -resistant isolates; however, much greater variability existed within the four resistant strains. The differences in PBP patterns included (1) electrophoretic mobility, (2) binding capacity for the antibiotic and (3) the presence of additional PBPs in two ofthe resistant isolates. However, decreased binding capacity was consistently demonstrated in PBP 5 (56 kDa) of all of the resistant isolates. Saturation curves with both penicillin and ampicillin indicated that PBP 5 had decreased affinity for the antibiotics. 'These results suggest ( a ) that care should be taken in interpreting changes in PBP profiles for species that demonstrate variability such as H . influenzae, and (b) that the decreased binding affinity of PBP 5 is a consistent finding associated with multiple ampicillin-resistant wild-type isolates.

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Two penicillin binding proteins of Haemophilus influenzae are lost after cells enter stationary phase

Cited by 9 publications

References 7 publications

The penicillin binding proteins of the genus Haemophilus

The penicillin binding proteins of the genus Haemophilus

Ampicillin Resistance and Penicillin-binding Proteins of Haemophilus influenzae

Penicillin-binding proteins 4 and 5 of Haemophilus influenzae are involved in cell wall incorporation

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