Speech restoration and complications of primary versus secondary tracheoesophageal puncture following total laryngectomy.

The tracheoesophageal (TE) fistula with a speech prosthesis has become the method of choice for vocal rehabilitation in many postlaryngectomy patients. Several modifications of the procedure have been described including primary TE puncture at the time of laryngectomy. Fear of increased risk of complications has kept the primary procedure from widespread usage. Our series of 95 TE fistula procedures from 1980 to 1988 revealed 33 to be primary and 62 secondary. Eighty-five percent (85%) (28 of 33) patients in the primary group achieved long-term satisfactory speech (1 year or more of follow-up). Complications occurred in 36% of this group of patients. The success rate for the secondary group was 69% (43 of 62), while the complication rate was 21%. There were no instances of death, sepsis, or mediastinitis associated with either primary or secondary TE fistula patients. It appears that the primary TE fistula can be performed as safely and effectively as the secondary procedure.

Strain distribution in extents of lysozyme resistance and O-acetylation of gonococcal peptidoglycan determined by high-performance liquid chromatography.

The extent of lysozyme resistance and O-acetylation of purified peptidoglycan (PG) from 20 strains of Neisseria gonorrhoeae was examined to determine how widespread these properties are among various subsets of gonococcal isolates. To determine digestibility by lysozyme, we treated [3H]- or [14C]glucosamine-labeled PG with hen egg white lysozyme (HEW-LZ) and determined the size distribution of HEW-LZ soluble PG at the completion of the reaction by molecular-sieve high-performance liquid chromatography, using a Varian TSK SW2000 column, a method that proved considerably more efficient than traditional chromatography for fractionating low-molecular-weight PG fragments solely on the basis of size. The extent of HEW-LZ resistance was expressed as the percentage of PG that was larger in size than disaccharide peptide tetramers (including insoluble PG removed by centrifugation). The percent O-acetylation was determined by converting insoluble PG totally to uncross-linked monomers by the combined action of Chalaropsis B muramidase followed by Escherichia coli endopeptidase and then quantitating radioactivity in O-acetylated and non-O-acetylated monomers after paper chromatography. The PG of the vast majority (19 of 20) of gonococcal strains examined was extensively HEW-LZ resistant (range, 40 to 60% larger than tetramers) and extensively O-acetylated (range, 34 to 52%). Only the PG of strain RD5 (highest rate of PG turnover among gonococci so far examined and the prototype of gonococci having O-acetyl-deficient PG) had greatly reduced O-acetylation (15%) and exhibited virtually no HEW-LZ resistance (2% larger than tetramers). Extensive HEW-LZ resistance and O-acetylation were apparently not associated specifically with (i) a given type of colonial variant (piliated versus nonpiliated or opaque versus transparent), (ii) a given type of clinical isolate (local versus disseminated), (iii) the extent of laboratory passage, or (iv) (with the possible exception of penicillin-resistant strain FA102) the presence of one or more genetic loci governing antibiotic resistance among members of an isogenic set of gonococci. From this survey, we conclude that lysozyme resistance and extensive O-acetylation of PG are widespread among gonococci and, thus, that most strains are potential sources of hydrolase-resistant PG that conceivably could persist as macromolecular fragments in vivo.

Resistance of O-acetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes.

Two naturally occurring forms of gonococcal peptidoglycan (PG) were tested for their susceptibility to human PG hydrolases. Purified 3H-labeled PG substituted extensively with O-acetyl derivatives (O-PG; from Neisseria gonorrhoeae FA19) and 14C-labeled O-acetyl-deficient PG (non-O-PG; from N. gonorrhoeae RD5) were mixed together and treated with either normal human sera (NHS) or with lysozyme purified from human polymorphonuclear leukocytes (PMN-LZ). The initial rate of hydrolysis of O-PG by NHS or by PMN-LZ was two- to fourfold less than that of its non-O-PG counterpart in the same tube. When the reactions were allowed to go to completion. NHS solubilized both PGs completely, whereas PMN-LZ solubilized all of the non-O-PG and left ca. 60% of the O-PG insoluble. The PMN-LZ-soluble fraction of O-PG consisted largely of glycosidically linked fragments with molecular weights greater than ca. 10(4), whereas the corresponding non-O-PG was degraded to lower-molecular-weight fragments, exclusively. At completion, NHS hydrolyzed both PGs to fragments whose size was equal to or smaller than that of the free disaccharide unit of PG, suggesting that human sera contain a peptide-splitting (amidase) activity and a glycosidase activity, in addition to that of the well-known muramidase. NHS also promoted the release of high-molecular-weight PG fragments from intact gonococci. The persistence of human hydrolase-resistant PG in the form of soluble macromolecular fragments may potentiate the biological effects of gonococcal PG in vivo.